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Information on EC 2.7.13.3 - histidine kinase
for references in articles please use BRENDA:EC2.7.13.3
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.13 Protein-histidine kinases
2.7.13.3 histidine kinase
IUBMB Comments
This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). A number of histones can act as acceptor.
The enzyme appears in viruses and cellular organisms
- 2.7.13.3
- autophosphorylation
- photoreceptors
-
far-red
- seedling
-
phosphorelay
- chromophore
-
perception
-
regulons
- hypocotyls
-
quorum
-
perceived
- pfr
-
chemoreceptor
-
senses
-
light-induced
- chey
-
flagellar
- synechocystis
-
etiolated
- caulobacter
-
photomorphogenesis
-
transmitter
-
quorum-sensing
-
fluence
- biliverdin
-
cryptochrome
- crescentus
-
methyl-accepting
-
dark-grown
- radiodurans
-
transphosphorylation
-
autoinducer
-
histidine-containing
-
chemosensory
-
photomorphogenic
-
extracytoplasmic
- arca
- deinococcus
- phototropins
- tetrapyrrole
- ompc
- c-di-gmp
-
diguanylate
- spo0a
-
four-helix
-
gravitropism
-
photoresponses
-
non-cognate
- xanthus
-
photoisomerization
- synthesis
- medicine
showSynonyms
histidine kinase, sensor kinase, sensor protein, phytochrome a, ethylene receptor, sensor histidine kinase, bacteriophytochrome, ornithine decarboxylase antizyme, chemotaxis protein, hybrid histidine kinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
33277 FimS
AaHSK1
aerobic respiration control sensor protein arcB
AHK
AHK5
alkaline phosphatase synthesis sensor protein phoR
AN4479.2
Arabidopsis histidine kinase
Arabidopsis histidine kinase 5
At2g47430
BA2291
BAB2_0652
BarA sensor kinase (sensory histidine kinase)
-
BinK
blue-light-activated histidine kinase
BOS1
BSU19190
BSU40400
C4-dicarboxylate transport sensor protein dctB
cbei2073
cbei4484
CheA
chemotaxis protein cheA
ChiS
Chk1p
CinS
CitA
CKI1
CKI1 histidine kinase
class I HK
class III HK
copper resistance, histidine kinase
-
CovS
CPR0195
CpxA
cytokinin independent I histidine kinase
cytokinin independent1
CzcS
DCC-1 protein
DctB
DcuS
DesK
development and carotenogenesis control-1 protein
DosT
Drak
DraK histidine kinase
ENVZ
ethylene receptor
ethylene resistant 1
-
the carboxyl-terminal part of ethylene resistant 1 consists of a histidine kinase domain and a response regulator domain
ETR1
EvgS
FimS
FimS histidine kinase
FrzE
GacS
Group III histidine kinase
Group III HK
group III two-component histidine kinase
-
heme-nitric oxide oxygen binding proteins-associated histidine kinase
-
-
high-affinity potassium transport system
-
Hik2
Hik34
HISTIDIN kinase (histidine protein kinase PlnB, sensor protein)
histidine autokinase
histidine kinase
histidine kinase CKI1
histidine kinase EnvZ
histidine kinase PilS
histidine kinase SasA
histidine protein kinase
histidine sensor kinase
HK1
HK2
HK853
HP0244
hybrid histidine kinase
HydH
iron-sensing histidine kinase
KINA
KinC
KinD
LOV
LOVHK
NCU00939
NikA
nitrate/nitrite sensor protein narQ
nitrate/nitrite sensor protein narX
nitrogen regulation protein NR(II)
nitrogen regulation protein ntrB
nitrogen regulation protein ntrY
nodulation protein V
NreB
ohkAsp
osmolarity sensor protein envZ
osmolarity two-component system protein SLN1
-
PA2524
PdhS
PGN_0904
PhoQ
phosphate regulon sensor protein phoR
phosphoglycerate transport system sensor protein pgtB
-
phytochrome-like protein cph1 (light-regulated histidine)
-
PleC
PleC-DivJ homolog sensor
PleCHKD
the PleC kinase domain has histidine kinase activity
RaxH
SaeS
SAOUHSC_00021
SasA
SCO3062
secretion system regulator:sensor component
-
SenS
sensor histidine kinase
sensor histidine kinase A
sensor histidine kinase D
sensor histidine kinase DesK
sensor histidine kinase mtrB
sensor kinase citA
sensor kinase cusS
sensor kinase dpiB
sensor protein atoS
sensor protein baeS
sensor protein barA
-
sensor protein basS/pmrB
sensor protein chvG
sensor protein chvG (histidine kinase sensory protein)
-
sensor protein citS
sensor protein cpxA
-
sensor protein creC
sensor protein czcS
sensor protein dcuS
sensor protein degS
sensor protein divL
sensor protein evgS precursor
sensor protein fixL
sensor protein irlS
sensor protein kdpD
sensor protein phoQ
sensor protein qseC
sensor protein rcsC (capsular synthesis regulator)
sensor protein resE
sensor protein roxS
sensor protein rstB
sensor protein torS
sensor protein uhpB
sensor protein zraS
sensor with histidine kinase
sensor-like histidine kinase senX3
sensory histidine kinase
sensory histidine kinase in two-component regulatory system with ArcA
-
sensory histidine kinase in two-component regulatory system with DcuR, senses fumarate/C4-dicarboxylate
-
sensory histidine kinase in two-component regulatory system with NarP
-
sensory kinase (alternative) in two-component regulatory system with CreB (or alternatively PhoB), senses catabolite repression
-
sensory kinase in multi-component regulatory system with TorR
-
sensory kinase in two-component regulatory system with CpxR, senses misfolded proteins in bacterial envelope
-
sensory kinase in two-component regulatory system with PhoB, regulates pho regulon
-
sensory kinase in two-component regulatory system wtih KdpE, regulates kdp operon
-
sensory transduction histidine kinase
sensory transduction protein kinase
Shk1
slr1147
sporulation kinase
sporulation kinase A (stage II sporulation protein J)
-
sporulation kinase D
SS1G_12694
stage 0 sporulation protein A homolog
subtilin biosynthesis sensor protein spaK
TcsC
tetrathionate reductase complex: sensory transduction histidine kinase
-
TMAO reductase S
TM_0853
TorS
transmembrane sensor histidine kinase transcription regulator protein
-
tricarboxylic transport: regulatory protein
-
trimethylamine-N-oxide reductase S
TWO component response regulator transcription regulator protein
-
two component system histidine kinase
two-component histidine kinase
two-component sensor kinase
-
two-component sensor kinase yesM
two-component system histidine kinase
VC0622
VC_0622
VF_A0360
VicK
VicK-like protein
VirA
virulence sensor protein bvgS precursor
virulence sensor protein phoQ
-
W83 FimS
WalK
wide host range virA protein (WHR virA)
YycG
YycG kinase
additional information
aerobic respiration control sensor protein arcB
-
alkaline phosphatase synthesis sensor protein phoR
-
C4-dicarboxylate transport sensor protein dctB
-
chemotaxis protein cheA
-
chemotaxis protein cheA
-
DctB
Vibrio cholerae serotype O1 MO45
-
-
-
FrzE
-
hybrid protein consisting of a CheA histidine kinase and a CheY receiver domain
HISTIDIN kinase (histidine protein kinase PlnB, sensor protein)
-
HISTIDIN kinase (histidine protein kinase PlnB, sensor protein)
-
-
histidine kinase
-
nitrate/nitrite sensor protein narQ
-
nitrate/nitrite sensor protein narX
-
-
nitrogen regulation protein NR(II)
-
nitrogen regulation protein NR(II)
-
osmolarity sensor protein envZ
-
osmolarity sensor protein envZ
-
osmolarity sensor protein envZ
-
sensor histidine kinase
two-component system formed by sensor histidine kinase and a response regulator
sensor histidine kinase
two-component system formed by sensor histidine kinase and a response regulator
-
sensor protein basS/pmrB
-
sensor protein evgS precursor
-
sensor protein rcsC (capsular synthesis regulator)
-
sensor protein rcsC (capsular synthesis regulator)
-
sensory transduction histidine kinase
-
sensory transduction protein kinase
-
virulence sensor protein bvgS precursor
-
additional information
-
AHK5 belongs to the the canonical HK class of proteins in Arabidopsis thaliana
additional information
DcuS is a member of the periplasmic sensing histidine kinases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
-
-
-
-
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
catalytic mechanism for Brucella LOV-HK, molecular modeling and simulations, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
phospho-group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:protein-L-histidine N-phosphotransferase
This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). A number of histones can act as acceptor.
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CAS REGISTRY NUMBER
COMMENTARY
99283-67-7
protein-histidine kinases, EC 2.7.13.1, EC 2.7.13.2, and EC 2.7.13.3 are not distinguished in Chemical Abstracts
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + CpdR-L-histidine
ADP + CpdR-N-phospho-L-histidine
-
Substrates: -
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ATP + CtrA-L-histidine
ADP + CtrA-N-phospho-L-histidine
-
Substrates: -
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ATP + DivK
?
-
Substrates: DivJ is the main kinase of DivK
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ATP + histidine kinase EnvZ
ADP + histidine kinase EnvZ N-phospho-L-histidine
Substrates: autophosphorylation. Probing catalytically essential domain orientation in histidine kinase EnvZ by targeted disulfide crosslinking
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ATP + Spo0F protein L-histidine
ADP + Spo0F protein N-phospho-L-histidine
-
Substrates: -
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ATP + VirG-L-histidine
ADP + VirG-N-phospho-L-histidine
-
Substrates: -
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CitB + ATP
?
Substrates: a fusion protein MalE-CitAC is composed of the maltose-binding protein and the CitA kinase domain shows constitutive autokinase activity and transfers the gamma-phosphate group of ATP to its cognate response regulator CitB
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DcuR + ATP
?
Substrates: the phosphoryl group of DcuS is rapidly transferred to the response regulator DcuR. Upon phosphorylation, DcuR binds specifically to dcuB promoter DNA
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EvgA + ATP
?
Substrates: one hybrid histidine kinase consisting of the BvgS transmitter and HPt domains and of the EvgS receiver domain BvgS-TO-EvgS-R is able to phosphorylate BvgA but not EvgA. In contrast, the hybrid protein consisting of the BvgS transmitter and the EvgS receiver and HPt domains BvgS-T-EvgS-RO is unable to phosphorylate BvgA but efficiently phosphorylates EvgA
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Rcp1 + ATP
?
Substrates: Cph1 is a light-regulated histidine kinase that mediates red, far-red reversible phosphorylation of the a small response regulator Rcp1
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TorR + ATP
?
Substrates: TorS is a sensor that contains three phosphorylation sites and transphosphorylates TorR via a four-step phosphorelay, His443 to Asp723 to His850 to Asp(TorR). TorS can dephosphorylate phospho-TorR when trimethylamine N-oxide is removed. Dephosphorylation probably occurs by a reverse phosphorelay, Asp(TorR) to His850 to Asp723
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ArcA + ATP
?
Substrates: ArcB undergoes autophosphorylation at the expense of ATP and subsequently transphosphorylates its cognate response regulator ArcA through a His to Asp to His to Asp phosphorelay pathway
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ArcA + ATP
?
Substrates: ArcB undergoes autophosphorylation at the expense of ATP and subsequently transphosphorylates its cognate response regulator ArcA through a His to Asp to His to Asp phosphorelay pathway
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ArcA + ATP
?
Substrates: the arcB gene encodes a sensor-regulator protein for anaerobic repression of the arc modulon
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ArcA + ATP
?
Substrates: the ArcB and ArcA proteins constitute a two-component signal transduction system that plays a broad role in transcriptional regulation. Under anoxic or environmentally reducing conditions, the sensor kinase ArcB is stimulated to autophosphorylate at the expense of ATP and subsequently transphosphorylates the response regulator ArcA
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ArcA + ATP
?
Substrates: phosphoryl group transfer from phosphorylated ArcB to ArcA, signal transmission occurs solely by His-Asp-His-Asp phosphorelay
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ATP + a protein
ADP + a phosphoprotein
Substrates: the two-component sensory transduction system chvG/chvI is required for virulence of Agrobacterium tumefaciens
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ATP + a protein
ADP + a phosphoprotein
Agrobacterium tumefaciens C58 / ATCC 33970
Substrates: the two-component sensory transduction system chvG/chvI is required for virulence of Agrobacterium tumefaciens
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ATP + a protein
ADP + a phosphoprotein
Substrates: kinase of the alternate pathway for phosphorylating the SpoOF protein
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ATP + a protein
ADP + a phosphoprotein
Substrates: the essential two-component regulatory system yycF/yycG modulates expression of the ftsAZ operon in Bacillus subtilis
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ATP + a protein
ADP + a phosphoprotein
Substrates: the two-component signal transduction system yycF/yycG is essential for growth of Bacillus subtilis
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ATP + a protein
ADP + a phosphoprotein
Substrates: regulation of the levels of OmpF and OmpC is normally controlled by a multicomponent signal-transducing regulatory pair of proteins, EnvZ and OmpR. The effect RprX and RprY have on OmpF expression is mediated at the level of transcription. Thus, RprX and RprY may be interfering with the normal regulation of OmpF by OmpR and EnvZ
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ATP + a protein
ADP + a phosphoprotein
Substrates: the tyrosine kinase DivL function in cell cycle and developmental regulation is mediated, at least in part, by the global response regulator CtrA, the enzyme is essential for cell viability and division
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ATP + a protein
ADP + a phosphoprotein
-
Substrates: the tyrosine kinase DivL function in cell cycle and developmental regulation is mediated, at least in part, by the global response regulator CtrA, the enzyme is essential for cell viability and division
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ATP + a protein
ADP + a phosphoprotein
Substrates: photosynthesis gene expression in Rhodobacter sphaeroides is controlled in part by the two-component regulatory system composed of a membrane-bound sensor kinase PrrB and a response regulator PrrA
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ATP + a protein
ADP + a phosphoprotein
Substrates: regB is part of a two-component system and encodes a sensor kinase involved in the global regulation of both anoxygenic light-dependent- and oxygenic light-independent CO2 fixation as well as anoxygenic photosystem biosynthesis
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ATP + a protein
ADP + a phosphoprotein
Substrates: enzyme is involved in chemotaxis
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ATP + a protein
ADP + a phosphoprotein
Substrates: PrrB is responsive to the removal of oxygen and functions through the response regulator PrrA. Together, prrB and prrA provide the major signal involved in synthesis of the specialized intracytoplasmic membrane, harboring components essential to the light reactions of photosynthesis. PrrB is a global regulator of photosynthesis gene expression
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ATP + a protein
ADP + a phosphoprotein
Substrates: the two-component regulatory system CzcS/CzcR is involved in transcriptional control of heavy-metal homoeostasis in Alcaligenes eutrophus
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ATP + a protein
ADP + a phosphoprotein
Substrates: Deinococcus radiodurans bacteriophytochrome functions as a light-regulated histidine kinase, which helps protect the bacterium from visible light
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ATP + a protein
ADP + a phosphoprotein
Substrates: the two-component regulatory system VanS-VanR activates a promoter used for cotranscription of the vanH, vanA, and vanX resistance genes
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ATP + a protein
ADP + a phosphoprotein
Substrates: the two-component regulatory system VanS-VanR activates a promoter used for cotranscription of the vanH, vanA, and vanX resistance genes
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ATP + a protein
ADP + a phosphoprotein
Substrates: enzyme is involved in signal transduction controlling chemotaxis
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ATP + a protein
ADP + a phosphoprotein
Substrates: enzyme is involved in chemotaxis
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ATP + a protein
ADP + a phosphoprotein
Substrates: enzyme is involved in chemotaxis
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ATP + a protein
ADP + a phosphoprotein
Substrates: enzyme is involved in early steps of competence regulation
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ATP + CovR L-histidine
ADP + CovR N-phospho-L-histidine
-
Substrates: -
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ATP + CovR L-histidine
ADP + CovR N-phospho-L-histidine
Streptococcus pyogenes MGAS2221
-
Substrates: -
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ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
Substrates: -
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ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
Substrates: autophosphorylation of DraK and subsequent phosphotransfer to its cognate response regulator protein DraR
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ATP + histidine kinase Hik34
ADP + histidine kinase Hik34 N-phospho-L-histidine
-
Substrates: histidine kinase Hik34 might negatively regulate the expression of certain heat shock genes that might by related to thermotolerance in Synechocystis
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ATP + histidine kinase Hik34
ADP + histidine kinase Hik34 N-phospho-L-histidine
-
Substrates: autophosphorylation, in vitro at physiological temperatures, but not at elevated temperatures, such as 44°C
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ATP + histidine kinase HK2
ADP + histidine kinase HK2 N-phospho-L-histidine
-
Substrates: -
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ATP + histidine kinase HK2
ADP + histidine kinase HK2 N-phospho-L-histidine
-
Substrates: -
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ATP + PhoN protein L-histidine
ADP + PhoN protein N-phospho-L-histidine
-
Substrates: -
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ATP + PhoN protein L-histidine
ADP + PhoN protein N-phospho-L-histidine
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Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: AtBphP1 contains a typical two-component histidine kinase domain at its C-terminus whose activity is repressed after photoconversion to Pfr
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: AtBphP2 is repressed after photoconversion to Pr
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: the two-component histidine kinase alrO117 is involved in heterocyst development
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: canonical histidine kinase activity of the transmitter domain of the ETR1 ethylene receptor from Arabidopsis is not required for signal transmission
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA4223 is capable of inducing sporulation in Bacillus anthracis
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA2291 acts as a phosphatase on the sporulation phosphorelay
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA1351
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA1356 is capable of inducing sporulation
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA5029
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA2636
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA3702
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA1478
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA2644
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinases DivJ and PleC initiate signal transduction pathways that regulate an early cell division cycle step and the gain of motility later in the Caulobacter crescentus cell cycle
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: RodK may regulate multiple temporally separated events during fruiting body formation including stimulation of early developmental gene expression, inhibition of A-signal production and inhibition of the intercellular C-signal transduction pathway
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: the gene-disrupted mutant is unable to produce normal mature fruiting bodies and produces fewer spores
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: induced by dehydration and CaCl2. NTHK2 possesses Ser/Thr kinase activity in presence of Mn2+ and histidine kinase activity in presence of Ca2+
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Streptococcus pyogenes MGAS2221
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Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: histidine kinase CikA resets the circadian clock
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: the circadian clock-associated histidine kinase SasA is necessary for rubustness of the circadian rhythm of gene expression and involved in clock output
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: the circadian clock-associated histidine kinase SasA is necessary for rubustness of the circadian rhythm of gene expression and involved in clock output
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: the two-component system of histidine kinase and response regulator, His33-Rre31, acts as transducer of hyperosmotic stress
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: the two-component systes of histidine kinase and response regulator, His34-Rre1, acts as transducer of hyperosmotic stress
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: the two-component system of histidine kinase and response regulator, His10-Rre3, acts as transducer of hyperosmotic stress
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: the three-component system of histidine kinases and response regulator, His16-Hik41-Rre17, acts as transducer of hyperosmotic stress
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: in Synechocystis sp. PCC 6803 four histidine kinases, Hik16, Hik33, Hik34, and Hik41, perceive and transduce salt signals. The Hik16/Hik41 system responds only to NaCl
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: in Synechocystis sp. PCC 6803 four histidine kinases, Hik16, Hik33, Hik34, and Hik41, perceive and transduce salt signals
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
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Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: the two active sites of CheA homodimers exhibit large differences in their interactions with ATP
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ATP + Spo0A L-histidine
ADP + Spo0A N-phospho-L-histidine
Substrates: -
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ATP + Spo0A L-histidine
ADP + Spo0A N-phospho-L-histidine
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ATP + Spo0A-L-histidine
ADP + Spo0A-N-phospho-L-histidine
Substrates: -
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ATP + Spo0A-L-histidine
ADP + Spo0A-N-phospho-L-histidine
Substrates: -
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ATP + VicR L-histidine
ADP + VicR N-phospho-L-histidine
Substrates: -
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ATP + VicR L-histidine
ADP + VicR N-phospho-L-histidine
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ATP + VicR protein L-histidine
ADP + VicR protein N-phospho-L-histidine
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ATP + VicR protein L-histidine
ADP + VicR protein N-phospho-L-histidine
Streptococcus pneumoniae D39 / ATCC 7466
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ATP + YycF
ADP + phospho-YycF
Substrates: the formation of the division septum is necessary for YycG phosphorylation of YycF
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ATP + YycF
ADP + phospho-YycF
Substrates: a response regulator/transcription factor
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BvgA + ATP
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Substrates: the phosphorylated, purified C-terminal domain alone is sufficient for phosphotransfer to BvgA
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BvgA + ATP
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Substrates: the cytoplasmic portion of BvgS ('BvgS)
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BvgA + ATP
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Substrates: one hybrid histidine kinase consisting of the BvgS transmitter and HPt domains and of the EvgS receiver domain BvgS-TO-EvgS-R is able to phosphorylate BvgA but not EvgA. In contrast, the hybrid protein consisting of the BvgS transmitter and the EvgS receiver and HPt domains BvgS-T-EvgS-RO is unable to phosphorylate BvgA but efficiently phosphorylates EvgA
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GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
Substrates: the enzyme is involved the transition between the vegetative cycle and sporulation, multiple sensor histidine kinases are induced to autophosphorylate in response to sporulation specific signals in the phosphorelay, the BA2291 protein may act as a phosphatase on the sporulation phosphorelay when present at elevated levels, overview
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GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
Substrates: BA2291 is absolutely specific for guanine nucleotides in both the forward and reverse reactions, nucleotide specificity of BA2291, overview
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GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
Substrates: the enzyme is involved the transition between the vegetative cycle and sporulation, multiple sensor histidine kinases are induced to autophosphorylate in response to sporulation specific signals in the phosphorelay, the BA2291 protein may act as a phosphatase on the sporulation phosphorelay when present at elevated levels, overview
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GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
Substrates: BA2291 is absolutely specific for guanine nucleotides in both the forward and reverse reactions, nucleotide specificity of BA2291, overview
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GTP + Spo0F L-histidine
GDP + Spo0F N-phospho-L-histidine
Substrates: a protein purified from Bacillus subtilis
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GTP + Spo0F L-histidine
GDP + Spo0F N-phospho-L-histidine
Substrates: a protein purified from Bacillus subtilis
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protein + ATP
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Substrates: the cytoplasmic portion of BvgS autophosphorylates with the gamma-phosphate from [gamma-32P]ATP
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protein + ATP
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Substrates: DivL protein is homologous to the ubiquitous bacterial histidine protein kinases, it differs from previously studied members of this protein kinase family in that it contains a tyrosine residue Tyr550 in the conserved H-box instead of a histidine residue, which is the expected site of autophosphorylation. DivL is autophosphorylated on Tyr-550 in vitro, and this tyrosine residue is essential for cell viability and regulation of the cell division cycle
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protein + ATP
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Substrates: DivL protein is homologous to the ubiquitous bacterial histidine protein kinases, it differs from previously studied members of this protein kinase family in that it contains a tyrosine residue Tyr550 in the conserved H-box instead of a histidine residue, which is the expected site of autophosphorylation. DivL is autophosphorylated on Tyr-550 in vitro, and this tyrosine residue is essential for cell viability and regulation of the cell division cycle
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protein + ATP
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Substrates: H243 is a site of autophosphorylation as well as transphosphorylation to the conserved D55 residue of response regulator OmpR
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protein + ATP
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Substrates: a model of the mechanism of FrzE phosphorylation: autophosphorylation initially occurs at a conserved His residue within the "CheA" domain and then, via an intramolecular transphosphorylation, is transferred to a conserved aspartate residue within the "CheY" domain
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regulator protein OmpR + ATP
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Substrates: H243 is the a site of autophosphorylation as well as transphosphorylation to the conserved D55 residue of response regulator OmpR
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additional information
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Substrates: it is proposed that VirA acts as an environmental sensor of plant-derived inducer molecules and transmits this information to the level of vir gene expression
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Substrates: it is proposed that VirA acts as an environmental sensor of plant-derived inducer molecules and transmits this information to the level of vir gene expression
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Substrates: membrane-bound sensor of plant signal molecules
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Substrates: membrane-bound sensor of plant signal molecules
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additional information
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Substrates: AaHSK1 may interact with AaHOG1 at post-translational levels
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Substrates: AaHSK1 may interact with AaHOG1 at post-translational levels
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Substrates: AaHSK1 may interact with AaHOG1 at post-translational levels
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additional information
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
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Substrates: histidine kinase domain and response regulator domain form a two-component system
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Substrates: histidine kinase domain and response regulator domain form a two-component system
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additional information
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Substrates: histidine kinase domain and response regulator domain form a two-component system
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additional information
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Substrates: histidine kinase domain and response regulator domain form a two-component system
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additional information
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Substrates: histidine kinase domain and response regulator domain form a two-component system
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additional information
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Substrates: histidine kinase domain and response regulator domain form a two-component system
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additional information
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Substrates: histidine kinase domain and response regulator domain form a two-component system
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additional information
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Substrates: histidine kinase domain and response regulator domain form a two-component system
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additional information
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Substrates: ETR1 acts as an ethylene receptor
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Substrates: ETR1 acts as an ethylene receptor
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Substrates: ETR1 acts as an ethylene receptor
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Substrates: ETR1 acts as an ethylene receptor
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Substrates: ETR1 acts as an ethylene receptor
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Substrates: ETR1 acts as an ethylene receptor
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additional information
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Substrates: histidine kinases are part of two-component signal transduction systems that act to integrate environmental stimuli into a cellular response via a phosphotransfer relay mechanism, e.g. involved in stomatal guard cell response to H2O2, regulation of the physiological function, overview
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additional information
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Substrates: the enzyme performs regulatory autophosphorylation
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additional information
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Substrates: CKI1 interacts with proteins AHP2 and AHP3, but CKI1 is incapable of binding to cytokinins
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additional information
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Substrates: CKI1 interacts with proteins AHP2 and AHP3, but CKI1 is incapable of binding to cytokinins
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additional information
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Substrates: the two-component regulatory system, NtrY/NtrX is involved in nitrogen fixation and metabolism. NtrY is likely to represent the transmembrane sensor protein element in a two-component regulatory system
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Substrates: genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay
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additional information
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Substrates: genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay
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Substrates: BA2291 performs GTP-dependent autophosphorylation
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additional information
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Substrates: BA2291 performs GTP-dependent autophosphorylation
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additional information
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Substrates: genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay
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Substrates: BA2291 performs GTP-dependent autophosphorylation
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Substrates: mediates the transfer of phosphate to the Spo0A and Spo0F sporulation regulatory proteins. Spo0F protein is a much better phosphoreceptor for this kinase than Spo0A protein in vitro
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Substrates: two-component regulatory system CssR-CssS, is required for the cell to survive the severe secretion stress caused by a combination of high-level production of the alpha-amylase AmyQ and reduced levels of the extracytoplasmic folding factor PrsA. The Css system is required to degrade misfolded exported proteins at the membrane-cell wall interface. CssS represents the first identified sensor for extracytoplasmic protein misfolding in a Gram-positive eubacterium
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additional information
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Substrates: the CitST two-component system regulates the expression of the Mg-citrate transporter in Bacillus subtilis
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additional information
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Substrates: mediates the transfer of phosphate to the Spo0A and Spo0F sporulation regulatory proteins
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additional information
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Substrates: the enzyme is a regulator of chemotaxis
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Substrates: the enzyme is a regulator of chemotaxis
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Substrates: enzyme is responsible for regulation of subtilin biosynthesis
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Substrates: enzyme is responsible for regulation of subtilin biosynthesis
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additional information
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Substrates: activation role for ResD, and to a lesser extent ResE, in global regulation of aerobic and anaerobic respiration in Bacillus subtilis
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Substrates: The sensor histidine kinase YycG acts in a two-component system with response regulator/transcription factor YycF in Bacillus subtilis controling the synthesis of autolysins and autolysin inhibitors, that function in cell wall remodelling and cell separation, YycG sensor histidine kinase is a component of and perceives infirmation at the division septum in growing cells constituting a positive feedback loop, that serves to co-ordinate cell division with cell wall homeostasis, overview
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additional information
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Substrates: The sensor histidine kinase YycG acts in a two-component system with response regulator/transcription factor YycF in Bacillus subtilis controling the synthesis of autolysins and autolysin inhibitors, that function in cell wall remodelling and cell separation, YycG sensor histidine kinase is a component of and perceives infirmation at the division septum in growing cells constituting a positive feedback loop, that serves to co-ordinate cell division with cell wall homeostasis, overview
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Substrates: the N-terminal Per-ARNT-Sim domain plays a critical role in the catalytic activity of this enzyme, a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking this domain
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Substrates: the N-terminal Per-ARNT-Sim domain plays a critical role in the catalytic activity of this enzyme, a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking this domain
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Substrates: KinA performs autophosphorylation
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Substrates: KinA performs autophosphorylation
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Substrates: the enzyme performs catalytic autophosphorylation, mechanism and kinetics, overview. DesK displays a compact structure at the ATP-binding pocket: the ATP lid loop is short with no secondary structural organization and becomes ordered upon ATP loading. Sequence conservation mapping onto the molecular surface, semi-flexible protein-protein docking simulations, and structure-based point mutagenesis present a specific domain-domain geometry during autophosphorylation catalysis. In vitro, DesKC catalyzes three different reactions depending on the phosphorylation states of the partners: its own phosphorylation, phosphotransfer to DesR, and dephosphorylation of phospho-DesR. Protein-protein docking and modelling of the enzyme in autophosphorylation state, residues involved in domain-domain interaction modulate catalysis, overview
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additional information
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Substrates: the enzyme performs catalytic autophosphorylation, mechanism and kinetics, overview. DesK displays a compact structure at the ATP-binding pocket: the ATP lid loop is short with no secondary structural organization and becomes ordered upon ATP loading. Sequence conservation mapping onto the molecular surface, semi-flexible protein-protein docking simulations, and structure-based point mutagenesis present a specific domain-domain geometry during autophosphorylation catalysis. In vitro, DesKC catalyzes three different reactions depending on the phosphorylation states of the partners: its own phosphorylation, phosphotransfer to DesR, and dephosphorylation of phospho-DesR. Protein-protein docking and modelling of the enzyme in autophosphorylation state, residues involved in domain-domain interaction modulate catalysis, overview
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additional information
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Substrates: YycG interacts with the latter stage cell division proteins DivIB, Pbp2B and FtsL
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Substrates: YycG interacts with the latter stage cell division proteins DivIB, Pbp2B and FtsL
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additional information
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Substrates: the N-terminal Per-ARNT-Sim domain plays a critical role in the catalytic activity of this enzyme, a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking this domain
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additional information
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Substrates: KinA performs autophosphorylation
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additional information
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Substrates: the enzyme performs catalytic autophosphorylation, mechanism and kinetics, overview. DesK displays a compact structure at the ATP-binding pocket: the ATP lid loop is short with no secondary structural organization and becomes ordered upon ATP loading. Sequence conservation mapping onto the molecular surface, semi-flexible protein-protein docking simulations, and structure-based point mutagenesis present a specific domain-domain geometry during autophosphorylation catalysis. In vitro, DesKC catalyzes three different reactions depending on the phosphorylation states of the partners: its own phosphorylation, phosphotransfer to DesR, and dephosphorylation of phospho-DesR. Protein-protein docking and modelling of the enzyme in autophosphorylation state, residues involved in domain-domain interaction modulate catalysis, overview
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additional information
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Substrates: YycG interacts with the latter stage cell division proteins DivIB, Pbp2B and FtsL
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Substrates: bvgS and bvgA control the expression of the virulence-associated genes in Bordetella species by a system similar to the two-component systems used by a variety of bacterial species to respond to environmental stimuli
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Substrates: NodV and NodW proteins are members of the family of two-component regulatory systems, NodV responds to an environmental stimulus and, after signal transduction, NodW may be required to positively regulate the transcription of one or several unknown genes involved in the nodulation process
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Substrates: the enzyme is a biological oxygen sensors that restricts the expression of specific genes to hypoxic conditions
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Substrates: the enzyme is a biological oxygen sensors that restricts the expression of specific genes to hypoxic conditions
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Substrates: FixL and FixJ proteins are members of the two-component sensor/regulator family
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Substrates: upon illumination in the presence of ATP, the enzyme undergoes autophosphorylation
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Substrates: LOVHK is able to phosphotransfer to the central regulator of the GSR system in Brucella, specific interaction with its cognate response regulators
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Substrates: LOVHK is able to phosphotransfer to the central regulator of the GSR system in Brucella, specific interaction with its cognate response regulators
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Substrates: LOVHK is able to phosphotransfer to the central regulator of the GSR system in Brucella, specific interaction with its cognate response regulators
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additional information
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Substrates: upon illumination in the presence of ATP, the enzyme undergoes autophosphorylation
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additional information
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Substrates: autophosphorylation occurs when the ATP molecule bound to the the catalytic and ATP-binding subdomain phosphorylates the histidine residue in the dimerization/histidine phosphoacceptor subdomain. Histidine kinase dimerization implies that the directionality of the autophosphorylation reaction can proceed either in a cis (intramolecular) or in a trans (intermolecular) manner. Autophosphorylation occurs in cis in the dimer. Intramolecular interactions in the enzyme, overview. Arg321 from the alpha2 helix of the dimerization/histidine phosphoacceptor subdomain contacts Glu384, Tyr383 and the gamma phosphate from non-hydrolyzable ATP analogue AMP-PCP, closing the binding pocket
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Substrates: the two-component regulatory system irlR-irlS is involved in invasion of eukaryotic cells and heavy-metal resistance in Burkholderia pseudomallei
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Substrates: the two-component regulatory system irlR-irlS is involved in invasion of eukaryotic cells and heavy-metal resistance in Burkholderia pseudomallei
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Substrates: Cek1p phosphorylation via Sho1p does not require histidine kinase Chk1p
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Substrates: Cek1p phosphorylation via Sho1p does not require histidine kinase Chk1p
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Substrates: measurement of the enzyme's ATPase activity
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additional information
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Substrates: measurement of the enzyme's ATPase activity
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Substrates: autophosphorylation of MtrB-Strep in proteoliposomes in the presence of ATP
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Substrates: Cm-ETR1 mRNA is very high in the seeds and placenta. Marked increase of Cm-ETR1 mRNA parallels climacteric ethylene production. Cm-ETR1 plays a specific role not only in ripening but also in the early development of melon fruit
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Substrates: Cm-ETR1 mRNA is very high in the seeds and placenta. Marked increase of Cm-ETR1 mRNA parallels climacteric ethylene production. Cm-ETR1 plays a specific role not only in ripening but also in the early development of melon fruit
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Substrates: the VanR B-VanS B two-component regulatory system activates a promoter located immediately downstream from the vanS B gene
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Substrates: the sensory histidine kinase acts in the two-component system with the response regulator as RR-HK17, EF1633-EF1632, in the regulation of ethanolamine utilization, which can be the sole carbon source for the organism, mechanism, overview
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Substrates: upon illumination in the presence of ATP, the enzyme undergoes autophosphorylation
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Substrates: BarA/UvrY system activated biofilm formation. UvrY resides downstream from csrA in a signaling pathway for csrB and CsrA stimulates UvrY-dependent activation of csrB expression by BarA-dependent and BarA-independent mechanisms
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Substrates: E. coli BarA-UvrY two-component system is required for efficient switching between glycolytic and gluconeogenic carbon sources
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Substrates: E. coli BarA-UvrY two-component system is required for efficient switching between glycolytic and gluconeogenic carbon sources
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Substrates: purified BarA protein is able to autophosphorylate when incubated with [gamma-(32)P]ATP but not with [alpha-(32)P]ATP or [gamma-(32)P]GTP. Phosphorylated BarA, in turn, acts as an efficient phosphoryl group donor to UvrY. BarA and UvrY constitute a new two-component system for gene regulation in Escherichia coli
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Substrates: purified BarA protein is able to autophosphorylate when incubated with [gamma-(32)P]ATP but not with [alpha-(32)P]ATP or [gamma-(32)P]GTP. Phosphorylated BarA, in turn, acts as an efficient phosphoryl group donor to UvrY. BarA and UvrY constitute a new two-component system for gene regulation in Escherichia coli
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Substrates: enzyme is involved in adaptive responses in E. coli
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Substrates: enzyme is involved in adaptive responses in E. coli
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Substrates: CpxA functions as a transmembrane sensory protein
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Substrates: EnvZ modulates expression of the ompF and ompC genes through phosphotransfer signal transduction in Escherichia coli
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Substrates: enzyme controls the osmoregulated biosynthesis of the porin proteins OmpF and OmpC
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Substrates: the enzyme plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions
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Substrates: the enzyme plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions
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Substrates: the enzyme plays an important role in coupling signals received from membrane-bound receptors to changes in the swimming behavior of the cells in order to respond appropriately to environmental signals
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Substrates: the enzyme plays an important role in coupling signals received from membrane-bound receptors to changes in the swimming behavior of the cells in order to respond appropriately to environmental signals
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Substrates: a complex of the proteins CheA (CheAL and CheAS) and CheW constitutes a functional unit that responds to the signaling state of the chemoreceptors. The autophosphorylation rate of CheAL is much greater when CheAL and CheAS are complexed with CheW. Moreover, the presence of mutant chemoreceptors that cause cells to tumble increases this rate. At wild-type levels of expression, the isolated CheAL/CheAS/CheW complex accounts for about 10% of the total number of CheAL, CheAS, and CheW molecules and exists in a 1:1:1 stoichiometry. This complex is also required for CheAL/CheAS and CheW binding to the phosphorylation substrate, CheY
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Substrates: the protein is involved in osmoregulation of OmpF and OmpC. EnvZ is considered to be an osmosensor which transmits signals across the membrane to OmpR, a transcriptional activator for ompF and ompC
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Substrates: UhpB and perhaps UhpC play both positive and negative roles in the control of uhpT transcription
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Substrates: enzyme has an enhancing effect on the transcription of phoA, primary function may not be connected to the phosphate regulon
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Substrates: RcsC is the sensor components of the two-component regulatory system which regulates expression of the slime polysaccharide colanic acid. rcs system is essential for expression of high levels of the group I capsular polysaccharide in lon+ E. coli K30
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Substrates: colanic acid capsule synthesis in Escherichia coli K-12 is regulated by RcsB and RcsC. RcsC acts as the sensor and RcsB acts as the receiver or effector to stimulate capsule synthesis from cps genes
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Substrates: the HydH/G system senses high periplasmic Zn2+ and Pb2+ concentrations and contributes to metal tolerance by activating the expression of zraP
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Substrates: narL and narX mediate nitrate induction of nitrate reductase synthesis and nitrate repression of fumarate reductase synthesis
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Substrates: enzyme is involved in signal transduction
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Substrates: either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12. NarQ and NarX may have subtle functional differences
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Substrates: narQ is a nitrate sensor for nitrate-dependent gene regulation in Escherichia coli
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Substrates: the two-component sensor-effector system KdpD /KdpE controls expression of the kdpABC operon
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Substrates: the two-component sensor-effector system KdpD /KdpE controls expression of the kdpABC operon
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Substrates: the two-component sensor-effector system KdpD /KdpE controls expression of the kdpABC operon
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Substrates: the TorS/TorR two-component system induces the expression of the tor structural operon encoding the trimethylamine N-oxide reductase respiratory system in response to substrate availability. TorS belongs to a sensor subfamily that includes a classical transmitter domain, a receiver, and a C-terminal alternative transmitter domain
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Substrates: TorS is a sensor that contains three phosphorylation sites and transphosphorylates TorR via a four-step phosphorelation, His443--Asp723--His850--Asp(TorR)
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Substrates: QseBC is a two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli strains EHEC and K-12
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Substrates: QseBC is a two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli strains EHEC and K-12
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Substrates: QseBC is a two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli strains EHEC and K-12
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Substrates: TorS mediates the induction of the tor structural genes in response to trimethylamine N-oxide
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Substrates: TorS mediates the induction of the tor structural genes in response to trimethylamine N-oxide
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Substrates: the two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C4-dicarboxylate metabolism in response to extracellular C4-dicarboxylates such as fumarate or succinate. The phosphoryl group of DcuS is rapidly transferred to the response regulator DcuR. Upon phosphorylation, DcuR binds specifically to dcuB promoter DNA
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Substrates: the two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C4-dicarboxylate metabolism in response to extracellular C4-dicarboxylates such as fumarate or succinate. The phosphoryl group of DcuS is rapidly transferred to the response regulator DcuR. Upon phosphorylation, DcuR binds specifically to dcuB promoter DNA
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Substrates: the genes encoding the anaerobic fumarate respiratory system are transcriptionally regulated by C4-dicarboxylates. The regulation is effected by a two-component regulatory system, DcuSR, consisting of a sensory histidine kinase DcuS and a response regulator DcuR
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Substrates: the genes encoding the anaerobic fumarate respiratory system are transcriptionally regulated by C4-dicarboxylates. The regulation is effected by a two-component regulatory system, DcuSR, consisting of a sensory histidine kinase DcuS and a response regulator DcuR
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Substrates: periplasmic loop of DcuS serves as a C4-dicarboxylate sensor. The cytosolic region of DcuS contains two domains: a central PAS domain possibly acting as a second sensory domain and a C-terminal transmitter domain
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Substrates: expression of cusC is induced by high concentrations of copper ions, the cusRS two-component signal transduction system is required for copper-induced expression of pcoE, a plasmid-borne gene from the E. coli copper resistance operon pco. The genes cusRS are also required for the copper-dependent expression of at least one chromosomal gene, designated cusC, which is allelic to the recently identified virulence gene ibeB in E. coli K1. The cus locus may comprise a copper ion efflux system
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Substrates: the antizyme is a bifunctional protein serving as both an inhibitor of polyamine biosynthesis as well as a transcriptional regulator of an as yet unknown set of genes
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Substrates: the antizyme is a bifunctional protein serving as both an inhibitor of polyamine biosynthesis as well as a transcriptional regulator of an as yet unknown set of genes
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Substrates: the two-component systemDpiA/DpiB is involved in regulation of plasmid inheritance
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Substrates: the two-component systemDpiA/DpiB is involved in regulation of plasmid inheritance
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Substrates: deletion of PilS results in a non-pilated phenotype
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Substrates: DcuS is the C4-dicarboxylate sensor of Escherichia coli catalyzing transmembrane sensing
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Substrates: a chemical or other stimulus is detected by the periplasmic sensor domain of a transmembrane histidine kinase sensor, which in turn relays a signal through a phosphotransfer cascade to the cognate cytoplasmic response regulator. Such systems lead ultimately to changes in gene expression or cell motility. Mechanisms of ligand binding and signal transduction through the cell membrane, overview
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Substrates: RcsC is the sensor components of the two-component regulatory system which regulates expression of the slime polysaccharide colanic acid. rcs system is essential for expression of high levels of the group I capsular polysaccharide in lon+ E. coli K30
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Substrates: the enzyme HP0244 is not only required to regulate flagellar gene expression via its cognate response regulator, HP0703, but also to generate a response to declining medium pH. Although not required for survival at pH 4.5, HP0244 is required for survival at pH 2.5, overview
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Substrates: the enzyme HP0244 is not only required to regulate flagellar gene expression via its cognate response regulator, HP0703, but also to generate a response to declining medium pH. Although not required for survival at pH 4.5, HP0244 is required for survival at pH 2.5, overview
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Substrates: the HydH/G system senses high periplasmic Zn2+ and Pb2+ concentrations and contributes to metal tolerance by activating the expression of zraP
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Substrates: enzyme is involved in regulation of the phosphate regulon
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Substrates: citrate, Na+, and oxygen exert their regulatory effects via the CitA/CitB system. In the presence of these signals, the citAB gene products induce their own synthesis. The positive autoregulation occurs via co-transcription of citAB with citS and oadGAB
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Substrates: citrate, Na+, and oxygen exert their regulatory effects via the CitA/CitB system. In the presence of these signals, the citAB gene products induce their own synthesis. The positive autoregulation occurs via co-transcription of citAB with citS and oadGAB
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Substrates: the periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor
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Substrates: the periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor
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Substrates: DNA sequences of plnB reveals that the product closely resembles members of bacterial two-component signal transduction systems. The finding that plnABCD are transcribed from a common promoter suggests that the biological role played by the bacteriocin is somehow related to the regulatory function of the two-component system located on the same operon
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Substrates: DNA sequences of plnB reveals that the product closely resembles members of bacterial two-component signal transduction systems. The finding that plnABCD are transcribed from a common promoter suggests that the biological role played by the bacteriocin is somehow related to the regulatory function of the two-component system located on the same operon
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Substrates: neither HK1 nor HK2 is able to autophosphorylate itself, HK1 is an ATP binding protein, acts as a functional kinase and phosphorylates HK2 by interacting with it, transfer of a phosphoryl group from HK2 to the response regulator TcrA
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Substrates: neither HK1 nor HK2 is able to autophosphorylate itself, HK1 is an ATP binding protein, acts as a functional kinase and phosphorylates HK2 by interacting with it, transfer of a phosphoryl group from HK2 to the response regulator TcrA
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Substrates: FrzE is a second messenger that relays information between the signaling protein FrzCD and the gliding motor
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Substrates: no autophosphorylation of wild-type, is caused by the rate of dephosphorylation being higher than the rate of autophosphorylation
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Substrates: Myxococcus xanthus undergoes a complex starvation-induced developmental program that results in cells forming multicellular fruiting bodies by aggregating into mounds and then differentiating into spores. This developmental program involves EspA, which plays a key role in the timing of expression of genes necessary for progression of cells through the developmental program, overview
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Substrates: Myxococcus xanthus undergoes a complex starvation-induced developmental program that results in cells forming multicellular fruiting bodies by aggregating into mounds and then differentiating into spores. This developmental program involves EspA, which plays a key role in the timing of expression of genes necessary for progression of cells through the developmental program, overview
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Substrates: FrzE autophosphorylates the kinase domain at His-49, and phosphoryl groups are transferred to aspartate residues (Asp-52 and Asp-220) in the two receiver domains of FrzA. The FrzE receiver domain inhibits autophosphorylation of the FrzE kinase domain
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Substrates: moxY is part of the two-component regulatory system controlling methanol dehydrogenase synthesis
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Substrates: PilS/PilR is a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa. PilS is a sensor protein which when stimulated by the appropriate environmental signals activates PilR through kinase activity. PilR then activates transcription of pilA, probably by interacting with RNA polymerase containing RpoN
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Substrates: PilS/PilR is a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa. PilS is a sensor protein which when stimulated by the appropriate environmental signals activates PilR through kinase activity. PilR then activates transcription of pilA, probably by interacting with RNA polymerase containing RpoN
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Substrates: the two-component regulatory system PfeR/PfeS is involved in the expression of the ferric enterobactin receptor PfeA
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Substrates: deletion of PilS results in a non-pilated phenotype
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Substrates: signal transduction mechanism in the bacteriophytochrome, overview
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Substrates: signal transduction mechanism in the bacteriophytochrome, overview
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Substrates: structure-function relationship: the bacteriophytochrome possesses a histidine kinase domain and undergoes conformational changes during photoconversion, local structural changes originating in the photosensory domain modulate interactions between long, crossdomain signaling helices at the dimer interface and are transmitted to the spatially distant effector domain, thereby regulating its histidine kinase activity, overview
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Substrates: structure-function relationship: the bacteriophytochrome possesses a histidine kinase domain and undergoes conformational changes during photoconversion, local structural changes originating in the photosensory domain modulate interactions between long, crossdomain signaling helices at the dimer interface and are transmitted to the spatially distant effector domain, thereby regulating its histidine kinase activity, overview
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Substrates: A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
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Substrates: A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
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Substrates: A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
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Substrates: a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
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Substrates: a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
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Substrates: a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
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Substrates: in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase. The enzyme performs autophosphorylation using ATP
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Substrates: in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase. The enzyme performs autophosphorylation using ATP
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Substrates: in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase. The enzyme performs autophosphorylation using ATP
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Substrates: The two-component system is implicated in redox signaling and cytochrome oxidase activity, in expression of the cell density-dependent gene ddcA and in bacterial colonization of plant surfaces. The RoxS/RoxR regulon includes genes involved in sugar and amino acid metabolism and the sulfur starvation response and elements of the respiratory chain (a cbb3 cytochrome oxidase, Fe-S clusters, and cytochrome c-related proteins) or genes participating in the maintenance of the redox balance. The RoxS/RoxR system controls a broad set of functions that have an influence on energy metabolism, such as formaldehyde and formate dehydrogenases.
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Substrates: The two-component system is implicated in redox signaling and cytochrome oxidase activity, in expression of the cell density-dependent gene ddcA and in bacterial colonization of plant surfaces. The RoxS/RoxR regulon includes genes involved in sugar and amino acid metabolism and the sulfur starvation response and elements of the respiratory chain (a cbb3 cytochrome oxidase, Fe-S clusters, and cytochrome c-related proteins) or genes participating in the maintenance of the redox balance. The RoxS/RoxR system controls a broad set of functions that have an influence on energy metabolism, such as formaldehyde and formate dehydrogenases.
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Substrates: significant number of genes are influenced directly or indirectly by the RoxSR two-component system. 173 genes are found showing reduced expression in EU58 (RoxSR mutant strain) in comparison to the wild type, whereas 84 genes are upregulated in the mutant
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Substrates: significant number of genes are influenced directly or indirectly by the RoxSR two-component system. 173 genes are found showing reduced expression in EU58 (RoxSR mutant strain) in comparison to the wild type, whereas 84 genes are upregulated in the mutant
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Substrates: The two-component system is implicated in redox signaling and cytochrome oxidase activity, in expression of the cell density-dependent gene ddcA and in bacterial colonization of plant surfaces. The RoxS/RoxR regulon includes genes involved in sugar and amino acid metabolism and the sulfur starvation response and elements of the respiratory chain (a cbb3 cytochrome oxidase, Fe-S clusters, and cytochrome c-related proteins) or genes participating in the maintenance of the redox balance. The RoxS/RoxR system controls a broad set of functions that have an influence on energy metabolism, such as formaldehyde and formate dehydrogenases.
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Substrates: significant number of genes are influenced directly or indirectly by the RoxSR two-component system. 173 genes are found showing reduced expression in EU58 (RoxSR mutant strain) in comparison to the wild type, whereas 84 genes are upregulated in the mutant
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Substrates: two-component regulatory system CopR/CopS is required for copper-inducible expression of the copper resistance operon
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Substrates: upon illumination in the presence of ATP, the enzyme undergoes autophosphorylation
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Substrates: upon illumination in the presence of ATP, the enzyme undergoes autophosphorylation
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Substrates: required for the activation of the C4-dicarboxylate transport structural gene dctA in free-living Rhizobium leguminosarum
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Substrates: the gene regulates transcription of the nifHDK operon and so limits the expression of nitrogen fixation activity to periods of low environmental concentrations of both oxygen and fixed nitrogen
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Substrates: role of the C-terminal domains in the photocycle of a light sensor histidine kinase Ppr having a photoactive yellow protein, PYP, domain as the photosensor domain, photocycles of the PYP domain of Ppr and of the full-length Ppr. The, overview
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Substrates: the two-component system regulates an osmosensing MAP kinase cascade
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Substrates: the two-component system regulates an osmosensing MAP kinase cascade
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Substrates: ompR-envZ is a two component regulatory system that plays an important role in the regulation of Vi polysaccharide synthesis in Salmonella typhi. One of the environmental signals for this regulation may be osmolarity
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Substrates: UhpB and perhaps UhpC play both positive and negative roles in the control of uhpT transcription
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Substrates: during bacterial chemotaxis, the binding of stimulatory ligands to chemoreceptors at the cell periphery leads to a response at the flagellar motor. Three proteins appear to be required for receptor-mediated control of swimming behavior, the products of the cheA, cheW, and cheY genes
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Substrates: during bacterial chemotaxis, the binding of stimulatory ligands to chemoreceptors at the cell periphery leads to a response at the flagellar motor. Three proteins appear to be required for receptor-mediated control of swimming behavior, the products of the cheA, cheW, and cheY genes
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additional information
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Substrates: enzyme is required for the proper expression of the outer membrane proteins OmpC and OmpF
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additional information
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Substrates: the two-component regulatory system phoP/phoQ controls Salmonella typhimurium virulence
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additional information
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Substrates: the PhoP-PhoQ system exerts a master regulatory function for preventing bacterial overgrowth within fibroblasts
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additional information
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Substrates: enzyme is involved in the regulation of expression of phosphoglycerate transport in Salmonella typhimurium. pgtB and pgtC genes are involved in the induction of the pgtP expression by modulating derepressor activity
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additional information
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Substrates: PgtB and PgtC polypeptides modulate PgtA activity
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additional information
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Substrates: enzyme is involved in regulation of the phosphate regulon
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additional information
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Substrates: regulation of nitrogen fixation genes in Rhizobium meliloti is mediated by two proteins, FixL and FixJ, in response to oxygen availability, oxygen sensor
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additional information
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Substrates: FixL senses an environmental signal and transduces it to FixJ, a transcriptional activator of nif and fix genes
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additional information
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Substrates: genes dctB and dctD form a two-component system which responds to the presence of C4-dicarboxylates to regulate expression of a transport protein encoded by dctA
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additional information
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Substrates: in free-living cells, the regulatory dctBD genes are absolutely required for the expression of the dctA gene
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additional information
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Substrates: dctB-encoded protein includes a putative periplasmic N-terminal domain that senses the presence of dicarboxylates and a C-terminal cytoplasmic domain that activates the dctD-encoded protein
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additional information
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Substrates: the ExoS-ChvI two-component regulatory system regulates succinoglycan production. ChvG is the sensor protein of the ChvG-ChvI two-component regulatory system
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additional information
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Substrates: the ExoS-ChvI two-component regulatory system regulates succinoglycan production. ChvG is the sensor protein of the ChvG-ChvI two-component regulatory system
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additional information
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Substrates: in vitro autokinase activity of recombinant truncated enzyme mutant AgrCTM5-6C in N,N-dimethyldodecylamine N-oxide proteoliposomes
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additional information
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Substrates: VicK performs autophosphorylation for self-activation. VicK can also act as a phosphatase dephosphorylating phosphorylated VicR
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additional information
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Substrates: VicK performs autophosphorylation for self-activation. VicK can also act as a phosphatase dephosphorylating phosphorylated VicR
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?
additional information
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Substrates: the two-component regulatory system afsQ1/afsQ2 is involved in secondary metabolism
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?
additional information
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Substrates: the cutR-cutS operon regulates copper metabolism in Streptomyces
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additional information
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Substrates: a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
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additional information
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Substrates: a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
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additional information
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Substrates: the SenS/SenR system of Streptomyces reticuli regulates the expression of the redox regulator FurS, the catalase-peroxidase CpeB and the heme-binding protein HbpS. SenS/SenR also participates in sensing redox changes, mediated by HbpS. The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner, presence of SenS/SenR leads to the synthesis of extracellular redox active proteins, overview
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additional information
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Substrates: SenS performs autophosphorylation. HbpS/SenS interaction analysis, overview
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additional information
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Substrates: the SenS/SenR system of Streptomyces reticuli regulates the expression of the redox regulator FurS, the catalase-peroxidase CpeB and the heme-binding protein HbpS. SenS/SenR also participates in sensing redox changes, mediated by HbpS. The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner, presence of SenS/SenR leads to the synthesis of extracellular redox active proteins, overview
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additional information
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Substrates: SenS performs autophosphorylation. HbpS/SenS interaction analysis, overview
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additional information
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Substrates: the enzyme is involved in chemical sensing
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additional information
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Substrates: interaction of Hik2 with Rre1 and RppA, usage of recombinant N-terminally MBP-tagged proteins purified from Escherichia coli expression host
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additional information
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Substrates: during autophosphorylation, histidine kinases catalyze transfer of only the gamma-phosphate from an ATP molecule to their conserved histidine residue
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additional information
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Substrates: autophosphorylation activity
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additional information
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Substrates: autophosphorylation activity
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Substrates: histidine kinase performs autophosphorylation. The His-containing substrate domain (P1) is sequestered by interactions that depend upon P1 of the adjacent subunit. Non-hydrolyzable ATP analogues (but not ATP or ADP) release P1 from the protein core (domains P3P4P5) and increase its mobility. Autophosphorylation is possible only when the subunit with a functional P4 domain trans phosphorylates a functional P1 domain of the opposing subunit
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additional information
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Substrates: the enzyme is involved in chemotaxis
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additional information
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Substrates: the enzyme is involved in regulation of density-dependent expression of luminescence in Vibrio harveyi
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additional information
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Substrates: the enzyme is involved in regulation of density-dependent expression of luminescence in Vibrio harveyi
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additional information
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Substrates: enzyme is involved in positive regulation of synthesis of extracellular enzymes and polysaccharide in Xanthomonas campestris pathovar campestris
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additional information
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Substrates: full-length His-RaxH shows autophosphorylation activities
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additional information
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Substrates: full-length His-RaxH shows autophosphorylation activities
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
Substrates: -
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?
ATP + histidine kinase Hik34
ADP + histidine kinase Hik34 N-phospho-L-histidine
-
Substrates: histidine kinase Hik34 might negatively regulate the expression of certain heat shock genes that might by related to thermotolerance in Synechocystis
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?
ATP + YycF
ADP + phospho-YycF
Substrates: the formation of the division septum is necessary for YycG phosphorylation of YycF
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?
Rcp1 + ATP
?
Substrates: Cph1 is a light-regulated histidine kinase that mediates red, far-red reversible phosphorylation of the a small response regulator Rcp1
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?
ArcA + ATP
?
Substrates: ArcB undergoes autophosphorylation at the expense of ATP and subsequently transphosphorylates its cognate response regulator ArcA through a His to Asp to His to Asp phosphorelay pathway
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?
ArcA + ATP
?
Substrates: the arcB gene encodes a sensor-regulator protein for anaerobic repression of the arc modulon
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ArcA + ATP
?
Substrates: the ArcB and ArcA proteins constitute a two-component signal transduction system that plays a broad role in transcriptional regulation. Under anoxic or environmentally reducing conditions, the sensor kinase ArcB is stimulated to autophosphorylate at the expense of ATP and subsequently transphosphorylates the response regulator ArcA
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?
ArcA + ATP
?
Substrates: phosphoryl group transfer from phosphorylated ArcB to ArcA, signal transmission occurs solely by His-Asp-His-Asp phosphorelay
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?
ATP + a protein
ADP + a phosphoprotein
Substrates: the two-component sensory transduction system chvG/chvI is required for virulence of Agrobacterium tumefaciens
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ATP + a protein
ADP + a phosphoprotein
Agrobacterium tumefaciens C58 / ATCC 33970
Substrates: the two-component sensory transduction system chvG/chvI is required for virulence of Agrobacterium tumefaciens
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ATP + a protein
ADP + a phosphoprotein
Substrates: kinase of the alternate pathway for phosphorylating the SpoOF protein
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ATP + a protein
ADP + a phosphoprotein
Substrates: the essential two-component regulatory system yycF/yycG modulates expression of the ftsAZ operon in Bacillus subtilis
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ATP + a protein
ADP + a phosphoprotein
Substrates: the two-component signal transduction system yycF/yycG is essential for growth of Bacillus subtilis
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ATP + a protein
ADP + a phosphoprotein
Substrates: regulation of the levels of OmpF and OmpC is normally controlled by a multicomponent signal-transducing regulatory pair of proteins, EnvZ and OmpR. The effect RprX and RprY have on OmpF expression is mediated at the level of transcription. Thus, RprX and RprY may be interfering with the normal regulation of OmpF by OmpR and EnvZ
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ATP + a protein
ADP + a phosphoprotein
Substrates: the tyrosine kinase DivL function in cell cycle and developmental regulation is mediated, at least in part, by the global response regulator CtrA, the enzyme is essential for cell viability and division
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ATP + a protein
ADP + a phosphoprotein
-
Substrates: the tyrosine kinase DivL function in cell cycle and developmental regulation is mediated, at least in part, by the global response regulator CtrA, the enzyme is essential for cell viability and division
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ATP + a protein
ADP + a phosphoprotein
Substrates: photosynthesis gene expression in Rhodobacter sphaeroides is controlled in part by the two-component regulatory system composed of a membrane-bound sensor kinase PrrB and a response regulator PrrA
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ATP + a protein
ADP + a phosphoprotein
Substrates: regB is part of a two-component system and encodes a sensor kinase involved in the global regulation of both anoxygenic light-dependent- and oxygenic light-independent CO2 fixation as well as anoxygenic photosystem biosynthesis
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ATP + a protein
ADP + a phosphoprotein
Substrates: enzyme is involved in chemotaxis
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ATP + a protein
ADP + a phosphoprotein
Substrates: PrrB is responsive to the removal of oxygen and functions through the response regulator PrrA. Together, prrB and prrA provide the major signal involved in synthesis of the specialized intracytoplasmic membrane, harboring components essential to the light reactions of photosynthesis. PrrB is a global regulator of photosynthesis gene expression
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ATP + a protein
ADP + a phosphoprotein
Substrates: the two-component regulatory system CzcS/CzcR is involved in transcriptional control of heavy-metal homoeostasis in Alcaligenes eutrophus
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ATP + a protein
ADP + a phosphoprotein
Substrates: Deinococcus radiodurans bacteriophytochrome functions as a light-regulated histidine kinase, which helps protect the bacterium from visible light
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ATP + a protein
ADP + a phosphoprotein
Substrates: the two-component regulatory system VanS-VanR activates a promoter used for cotranscription of the vanH, vanA, and vanX resistance genes
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ATP + a protein
ADP + a phosphoprotein
Substrates: the two-component regulatory system VanS-VanR activates a promoter used for cotranscription of the vanH, vanA, and vanX resistance genes
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ATP + a protein
ADP + a phosphoprotein
Substrates: enzyme is involved in signal transduction controlling chemotaxis
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ATP + a protein
ADP + a phosphoprotein
Substrates: enzyme is involved in chemotaxis
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ATP + a protein
ADP + a phosphoprotein
Substrates: enzyme is involved in chemotaxis
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ATP + a protein
ADP + a phosphoprotein
Substrates: enzyme is involved in early steps of competence regulation
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ATP + CovR L-histidine
ADP + CovR N-phospho-L-histidine
-
Substrates: -
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?
ATP + CovR L-histidine
ADP + CovR N-phospho-L-histidine
Streptococcus pyogenes MGAS2221
-
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: AtBphP1 contains a typical two-component histidine kinase domain at its C-terminus whose activity is repressed after photoconversion to Pfr
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: AtBphP2 is repressed after photoconversion to Pr
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: the two-component histidine kinase alrO117 is involved in heterocyst development
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: canonical histidine kinase activity of the transmitter domain of the ETR1 ethylene receptor from Arabidopsis is not required for signal transmission
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA4223 is capable of inducing sporulation in Bacillus anthracis
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA2291 acts as a phosphatase on the sporulation phosphorelay
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA1351
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA1356 is capable of inducing sporulation
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA5029
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA2636
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA3702
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA1478
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase BA2644
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinases DivJ and PleC initiate signal transduction pathways that regulate an early cell division cycle step and the gain of motility later in the Caulobacter crescentus cell cycle
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: RodK may regulate multiple temporally separated events during fruiting body formation including stimulation of early developmental gene expression, inhibition of A-signal production and inhibition of the intercellular C-signal transduction pathway
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: the gene-disrupted mutant is unable to produce normal mature fruiting bodies and produces fewer spores
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: induced by dehydration and CaCl2. NTHK2 possesses Ser/Thr kinase activity in presence of Mn2+ and histidine kinase activity in presence of Ca2+
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: -
Products: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
Products: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
Products: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: -
Products: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Streptococcus pyogenes MGAS2221
-
Substrates: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
Products: -
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: histidine kinase CikA resets the circadian clock
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: the circadian clock-associated histidine kinase SasA is necessary for rubustness of the circadian rhythm of gene expression and involved in clock output
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: the circadian clock-associated histidine kinase SasA is necessary for rubustness of the circadian rhythm of gene expression and involved in clock output
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: the two-component system of histidine kinase and response regulator, His33-Rre31, acts as transducer of hyperosmotic stress
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: the two-component systes of histidine kinase and response regulator, His34-Rre1, acts as transducer of hyperosmotic stress
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: the two-component system of histidine kinase and response regulator, His10-Rre3, acts as transducer of hyperosmotic stress
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: the three-component system of histidine kinases and response regulator, His16-Hik41-Rre17, acts as transducer of hyperosmotic stress
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: in Synechocystis sp. PCC 6803 four histidine kinases, Hik16, Hik33, Hik34, and Hik41, perceive and transduce salt signals. The Hik16/Hik41 system responds only to NaCl
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: in Synechocystis sp. PCC 6803 four histidine kinases, Hik16, Hik33, Hik34, and Hik41, perceive and transduce salt signals
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ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
Products: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
Substrates: -
Products: -
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
Substrates: -
Products: -
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?
ATP + Spo0A L-histidine
ADP + Spo0A N-phospho-L-histidine
Substrates: -
Products: -
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?
ATP + Spo0A L-histidine
ADP + Spo0A N-phospho-L-histidine
Substrates: -
Products: -
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?
ATP + VicR L-histidine
ADP + VicR N-phospho-L-histidine
Substrates: -
Products: -
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?
ATP + VicR L-histidine
ADP + VicR N-phospho-L-histidine
Substrates: -
Products: -
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GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
Substrates: the enzyme is involved the transition between the vegetative cycle and sporulation, multiple sensor histidine kinases are induced to autophosphorylate in response to sporulation specific signals in the phosphorelay, the BA2291 protein may act as a phosphatase on the sporulation phosphorelay when present at elevated levels, overview
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GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
Substrates: the enzyme is involved the transition between the vegetative cycle and sporulation, multiple sensor histidine kinases are induced to autophosphorylate in response to sporulation specific signals in the phosphorelay, the BA2291 protein may act as a phosphatase on the sporulation phosphorelay when present at elevated levels, overview
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r
GTP + Spo0F L-histidine
GDP + Spo0F N-phospho-L-histidine
Substrates: a protein purified from Bacillus subtilis
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r
GTP + Spo0F L-histidine
GDP + Spo0F N-phospho-L-histidine
Substrates: a protein purified from Bacillus subtilis
Products: -
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r
additional information
?
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Substrates: it is proposed that VirA acts as an environmental sensor of plant-derived inducer molecules and transmits this information to the level of vir gene expression
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additional information
?
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Substrates: it is proposed that VirA acts as an environmental sensor of plant-derived inducer molecules and transmits this information to the level of vir gene expression
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additional information
?
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Substrates: membrane-bound sensor of plant signal molecules
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?
additional information
?
-
Substrates: membrane-bound sensor of plant signal molecules
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additional information
?
-
Substrates: AaHSK1 may interact with AaHOG1 at post-translational levels
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additional information
?
-
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Substrates: AaHSK1 may interact with AaHOG1 at post-translational levels
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additional information
?
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Substrates: AaHSK1 may interact with AaHOG1 at post-translational levels
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additional information
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
?
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
?
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
Products: -
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additional information
?
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
Products: -
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additional information
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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Substrates: AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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Substrates: ETR1 acts as an ethylene receptor
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Substrates: ETR1 acts as an ethylene receptor
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Substrates: ETR1 acts as an ethylene receptor
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Substrates: ETR1 acts as an ethylene receptor
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Substrates: ETR1 acts as an ethylene receptor
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Substrates: ETR1 acts as an ethylene receptor
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Substrates: histidine kinases are part of two-component signal transduction systems that act to integrate environmental stimuli into a cellular response via a phosphotransfer relay mechanism, e.g. involved in stomatal guard cell response to H2O2, regulation of the physiological function, overview
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Substrates: CKI1 interacts with proteins AHP2 and AHP3, but CKI1 is incapable of binding to cytokinins
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Substrates: CKI1 interacts with proteins AHP2 and AHP3, but CKI1 is incapable of binding to cytokinins
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Substrates: the two-component regulatory system, NtrY/NtrX is involved in nitrogen fixation and metabolism. NtrY is likely to represent the transmembrane sensor protein element in a two-component regulatory system
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Substrates: genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay
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Substrates: genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay
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Substrates: genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay
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Substrates: two-component regulatory system CssR-CssS, is required for the cell to survive the severe secretion stress caused by a combination of high-level production of the alpha-amylase AmyQ and reduced levels of the extracytoplasmic folding factor PrsA. The Css system is required to degrade misfolded exported proteins at the membrane-cell wall interface. CssS represents the first identified sensor for extracytoplasmic protein misfolding in a Gram-positive eubacterium
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Substrates: the CitST two-component system regulates the expression of the Mg-citrate transporter in Bacillus subtilis
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Substrates: mediates the transfer of phosphate to the Spo0A and Spo0F sporulation regulatory proteins
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Substrates: the enzyme is a regulator of chemotaxis
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Substrates: the enzyme is a regulator of chemotaxis
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Substrates: enzyme is responsible for regulation of subtilin biosynthesis
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Substrates: enzyme is responsible for regulation of subtilin biosynthesis
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Substrates: activation role for ResD, and to a lesser extent ResE, in global regulation of aerobic and anaerobic respiration in Bacillus subtilis
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Substrates: The sensor histidine kinase YycG acts in a two-component system with response regulator/transcription factor YycF in Bacillus subtilis controling the synthesis of autolysins and autolysin inhibitors, that function in cell wall remodelling and cell separation, YycG sensor histidine kinase is a component of and perceives infirmation at the division septum in growing cells constituting a positive feedback loop, that serves to co-ordinate cell division with cell wall homeostasis, overview
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Substrates: The sensor histidine kinase YycG acts in a two-component system with response regulator/transcription factor YycF in Bacillus subtilis controling the synthesis of autolysins and autolysin inhibitors, that function in cell wall remodelling and cell separation, YycG sensor histidine kinase is a component of and perceives infirmation at the division septum in growing cells constituting a positive feedback loop, that serves to co-ordinate cell division with cell wall homeostasis, overview
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Substrates: the N-terminal Per-ARNT-Sim domain plays a critical role in the catalytic activity of this enzyme, a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking this domain
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Substrates: the N-terminal Per-ARNT-Sim domain plays a critical role in the catalytic activity of this enzyme, a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking this domain
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Substrates: the N-terminal Per-ARNT-Sim domain plays a critical role in the catalytic activity of this enzyme, a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking this domain
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Substrates: bvgS and bvgA control the expression of the virulence-associated genes in Bordetella species by a system similar to the two-component systems used by a variety of bacterial species to respond to environmental stimuli
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Substrates: NodV and NodW proteins are members of the family of two-component regulatory systems, NodV responds to an environmental stimulus and, after signal transduction, NodW may be required to positively regulate the transcription of one or several unknown genes involved in the nodulation process
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Substrates: the enzyme is a biological oxygen sensors that restricts the expression of specific genes to hypoxic conditions
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Substrates: the enzyme is a biological oxygen sensors that restricts the expression of specific genes to hypoxic conditions
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Substrates: FixL and FixJ proteins are members of the two-component sensor/regulator family
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Substrates: LOVHK is able to phosphotransfer to the central regulator of the GSR system in Brucella, specific interaction with its cognate response regulators
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Substrates: LOVHK is able to phosphotransfer to the central regulator of the GSR system in Brucella, specific interaction with its cognate response regulators
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Substrates: LOVHK is able to phosphotransfer to the central regulator of the GSR system in Brucella, specific interaction with its cognate response regulators
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Substrates: the two-component regulatory system irlR-irlS is involved in invasion of eukaryotic cells and heavy-metal resistance in Burkholderia pseudomallei
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Substrates: the two-component regulatory system irlR-irlS is involved in invasion of eukaryotic cells and heavy-metal resistance in Burkholderia pseudomallei
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Substrates: Cm-ETR1 mRNA is very high in the seeds and placenta. Marked increase of Cm-ETR1 mRNA parallels climacteric ethylene production. Cm-ETR1 plays a specific role not only in ripening but also in the early development of melon fruit
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Substrates: Cm-ETR1 mRNA is very high in the seeds and placenta. Marked increase of Cm-ETR1 mRNA parallels climacteric ethylene production. Cm-ETR1 plays a specific role not only in ripening but also in the early development of melon fruit
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Substrates: the VanR B-VanS B two-component regulatory system activates a promoter located immediately downstream from the vanS B gene
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Substrates: the sensory histidine kinase acts in the two-component system with the response regulator as RR-HK17, EF1633-EF1632, in the regulation of ethanolamine utilization, which can be the sole carbon source for the organism, mechanism, overview
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Substrates: BarA/UvrY system activated biofilm formation. UvrY resides downstream from csrA in a signaling pathway for csrB and CsrA stimulates UvrY-dependent activation of csrB expression by BarA-dependent and BarA-independent mechanisms
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Substrates: E. coli BarA-UvrY two-component system is required for efficient switching between glycolytic and gluconeogenic carbon sources
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Substrates: E. coli BarA-UvrY two-component system is required for efficient switching between glycolytic and gluconeogenic carbon sources
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Substrates: purified BarA protein is able to autophosphorylate when incubated with [gamma-(32)P]ATP but not with [alpha-(32)P]ATP or [gamma-(32)P]GTP. Phosphorylated BarA, in turn, acts as an efficient phosphoryl group donor to UvrY. BarA and UvrY constitute a new two-component system for gene regulation in Escherichia coli
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Substrates: purified BarA protein is able to autophosphorylate when incubated with [gamma-(32)P]ATP but not with [alpha-(32)P]ATP or [gamma-(32)P]GTP. Phosphorylated BarA, in turn, acts as an efficient phosphoryl group donor to UvrY. BarA and UvrY constitute a new two-component system for gene regulation in Escherichia coli
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Substrates: enzyme is involved in adaptive responses in E. coli
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Substrates: enzyme is involved in adaptive responses in E. coli
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Substrates: CpxA functions as a transmembrane sensory protein
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Substrates: EnvZ modulates expression of the ompF and ompC genes through phosphotransfer signal transduction in Escherichia coli
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Substrates: enzyme controls the osmoregulated biosynthesis of the porin proteins OmpF and OmpC
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Substrates: the enzyme plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions
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Substrates: the enzyme plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions
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Substrates: the enzyme plays an important role in coupling signals received from membrane-bound receptors to changes in the swimming behavior of the cells in order to respond appropriately to environmental signals
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Substrates: the enzyme plays an important role in coupling signals received from membrane-bound receptors to changes in the swimming behavior of the cells in order to respond appropriately to environmental signals
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Substrates: a complex of the proteins CheA (CheAL and CheAS) and CheW constitutes a functional unit that responds to the signaling state of the chemoreceptors. The autophosphorylation rate of CheAL is much greater when CheAL and CheAS are complexed with CheW. Moreover, the presence of mutant chemoreceptors that cause cells to tumble increases this rate. At wild-type levels of expression, the isolated CheAL/CheAS/CheW complex accounts for about 10% of the total number of CheAL, CheAS, and CheW molecules and exists in a 1:1:1 stoichiometry. This complex is also required for CheAL/CheAS and CheW binding to the phosphorylation substrate, CheY
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Substrates: the protein is involved in osmoregulation of OmpF and OmpC. EnvZ is considered to be an osmosensor which transmits signals across the membrane to OmpR, a transcriptional activator for ompF and ompC
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Substrates: UhpB and perhaps UhpC play both positive and negative roles in the control of uhpT transcription
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Substrates: enzyme has an enhancing effect on the transcription of phoA, primary function may not be connected to the phosphate regulon
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Substrates: RcsC is the sensor components of the two-component regulatory system which regulates expression of the slime polysaccharide colanic acid. rcs system is essential for expression of high levels of the group I capsular polysaccharide in lon+ E. coli K30
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Substrates: colanic acid capsule synthesis in Escherichia coli K-12 is regulated by RcsB and RcsC. RcsC acts as the sensor and RcsB acts as the receiver or effector to stimulate capsule synthesis from cps genes
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Substrates: the HydH/G system senses high periplasmic Zn2+ and Pb2+ concentrations and contributes to metal tolerance by activating the expression of zraP
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Substrates: narL and narX mediate nitrate induction of nitrate reductase synthesis and nitrate repression of fumarate reductase synthesis
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Substrates: enzyme is involved in signal transduction
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Substrates: either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12. NarQ and NarX may have subtle functional differences
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Substrates: narQ is a nitrate sensor for nitrate-dependent gene regulation in Escherichia coli
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Substrates: the two-component sensor-effector system KdpD /KdpE controls expression of the kdpABC operon
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Substrates: the two-component sensor-effector system KdpD /KdpE controls expression of the kdpABC operon
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Substrates: the two-component sensor-effector system KdpD /KdpE controls expression of the kdpABC operon
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Substrates: the TorS/TorR two-component system induces the expression of the tor structural operon encoding the trimethylamine N-oxide reductase respiratory system in response to substrate availability. TorS belongs to a sensor subfamily that includes a classical transmitter domain, a receiver, and a C-terminal alternative transmitter domain
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Substrates: TorS is a sensor that contains three phosphorylation sites and transphosphorylates TorR via a four-step phosphorelation, His443--Asp723--His850--Asp(TorR)
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Substrates: QseBC is a two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli strains EHEC and K-12
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Substrates: QseBC is a two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli strains EHEC and K-12
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Substrates: QseBC is a two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli strains EHEC and K-12
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Substrates: TorS mediates the induction of the tor structural genes in response to trimethylamine N-oxide
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Substrates: TorS mediates the induction of the tor structural genes in response to trimethylamine N-oxide
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Substrates: the two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C4-dicarboxylate metabolism in response to extracellular C4-dicarboxylates such as fumarate or succinate. The phosphoryl group of DcuS is rapidly transferred to the response regulator DcuR. Upon phosphorylation, DcuR binds specifically to dcuB promoter DNA
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Substrates: the two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C4-dicarboxylate metabolism in response to extracellular C4-dicarboxylates such as fumarate or succinate. The phosphoryl group of DcuS is rapidly transferred to the response regulator DcuR. Upon phosphorylation, DcuR binds specifically to dcuB promoter DNA
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Substrates: the genes encoding the anaerobic fumarate respiratory system are transcriptionally regulated by C4-dicarboxylates. The regulation is effected by a two-component regulatory system, DcuSR, consisting of a sensory histidine kinase DcuS and a response regulator DcuR
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Substrates: the genes encoding the anaerobic fumarate respiratory system are transcriptionally regulated by C4-dicarboxylates. The regulation is effected by a two-component regulatory system, DcuSR, consisting of a sensory histidine kinase DcuS and a response regulator DcuR
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Substrates: periplasmic loop of DcuS serves as a C4-dicarboxylate sensor. The cytosolic region of DcuS contains two domains: a central PAS domain possibly acting as a second sensory domain and a C-terminal transmitter domain
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Substrates: expression of cusC is induced by high concentrations of copper ions, the cusRS two-component signal transduction system is required for copper-induced expression of pcoE, a plasmid-borne gene from the E. coli copper resistance operon pco. The genes cusRS are also required for the copper-dependent expression of at least one chromosomal gene, designated cusC, which is allelic to the recently identified virulence gene ibeB in E. coli K1. The cus locus may comprise a copper ion efflux system
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Substrates: the antizyme is a bifunctional protein serving as both an inhibitor of polyamine biosynthesis as well as a transcriptional regulator of an as yet unknown set of genes
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Substrates: the antizyme is a bifunctional protein serving as both an inhibitor of polyamine biosynthesis as well as a transcriptional regulator of an as yet unknown set of genes
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Substrates: the two-component systemDpiA/DpiB is involved in regulation of plasmid inheritance
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Substrates: the two-component systemDpiA/DpiB is involved in regulation of plasmid inheritance
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Substrates: deletion of PilS results in a non-pilated phenotype
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Substrates: DcuS is the C4-dicarboxylate sensor of Escherichia coli catalyzing transmembrane sensing
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Substrates: a chemical or other stimulus is detected by the periplasmic sensor domain of a transmembrane histidine kinase sensor, which in turn relays a signal through a phosphotransfer cascade to the cognate cytoplasmic response regulator. Such systems lead ultimately to changes in gene expression or cell motility. Mechanisms of ligand binding and signal transduction through the cell membrane, overview
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Substrates: RcsC is the sensor components of the two-component regulatory system which regulates expression of the slime polysaccharide colanic acid. rcs system is essential for expression of high levels of the group I capsular polysaccharide in lon+ E. coli K30
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Substrates: the enzyme HP0244 is not only required to regulate flagellar gene expression via its cognate response regulator, HP0703, but also to generate a response to declining medium pH. Although not required for survival at pH 4.5, HP0244 is required for survival at pH 2.5, overview
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Substrates: the enzyme HP0244 is not only required to regulate flagellar gene expression via its cognate response regulator, HP0703, but also to generate a response to declining medium pH. Although not required for survival at pH 4.5, HP0244 is required for survival at pH 2.5, overview
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Substrates: the HydH/G system senses high periplasmic Zn2+ and Pb2+ concentrations and contributes to metal tolerance by activating the expression of zraP
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Substrates: enzyme is involved in regulation of the phosphate regulon
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Substrates: citrate, Na+, and oxygen exert their regulatory effects via the CitA/CitB system. In the presence of these signals, the citAB gene products induce their own synthesis. The positive autoregulation occurs via co-transcription of citAB with citS and oadGAB
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Substrates: citrate, Na+, and oxygen exert their regulatory effects via the CitA/CitB system. In the presence of these signals, the citAB gene products induce their own synthesis. The positive autoregulation occurs via co-transcription of citAB with citS and oadGAB
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Substrates: the periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor
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Substrates: the periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor
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Substrates: DNA sequences of plnB reveals that the product closely resembles members of bacterial two-component signal transduction systems. The finding that plnABCD are transcribed from a common promoter suggests that the biological role played by the bacteriocin is somehow related to the regulatory function of the two-component system located on the same operon
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Substrates: DNA sequences of plnB reveals that the product closely resembles members of bacterial two-component signal transduction systems. The finding that plnABCD are transcribed from a common promoter suggests that the biological role played by the bacteriocin is somehow related to the regulatory function of the two-component system located on the same operon
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Substrates: FrzE is a second messenger that relays information between the signaling protein FrzCD and the gliding motor
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Substrates: Myxococcus xanthus undergoes a complex starvation-induced developmental program that results in cells forming multicellular fruiting bodies by aggregating into mounds and then differentiating into spores. This developmental program involves EspA, which plays a key role in the timing of expression of genes necessary for progression of cells through the developmental program, overview
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Substrates: Myxococcus xanthus undergoes a complex starvation-induced developmental program that results in cells forming multicellular fruiting bodies by aggregating into mounds and then differentiating into spores. This developmental program involves EspA, which plays a key role in the timing of expression of genes necessary for progression of cells through the developmental program, overview
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Substrates: moxY is part of the two-component regulatory system controlling methanol dehydrogenase synthesis
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Substrates: PilS/PilR is a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa. PilS is a sensor protein which when stimulated by the appropriate environmental signals activates PilR through kinase activity. PilR then activates transcription of pilA, probably by interacting with RNA polymerase containing RpoN
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Substrates: PilS/PilR is a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa. PilS is a sensor protein which when stimulated by the appropriate environmental signals activates PilR through kinase activity. PilR then activates transcription of pilA, probably by interacting with RNA polymerase containing RpoN
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Substrates: the two-component regulatory system PfeR/PfeS is involved in the expression of the ferric enterobactin receptor PfeA
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Substrates: deletion of PilS results in a non-pilated phenotype
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Substrates: signal transduction mechanism in the bacteriophytochrome, overview
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Substrates: signal transduction mechanism in the bacteriophytochrome, overview
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Substrates: A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
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Substrates: A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
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Substrates: A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
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additional information
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Substrates: a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
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additional information
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Substrates: a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
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additional information
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Substrates: a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
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additional information
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Substrates: The two-component system is implicated in redox signaling and cytochrome oxidase activity, in expression of the cell density-dependent gene ddcA and in bacterial colonization of plant surfaces. The RoxS/RoxR regulon includes genes involved in sugar and amino acid metabolism and the sulfur starvation response and elements of the respiratory chain (a cbb3 cytochrome oxidase, Fe-S clusters, and cytochrome c-related proteins) or genes participating in the maintenance of the redox balance. The RoxS/RoxR system controls a broad set of functions that have an influence on energy metabolism, such as formaldehyde and formate dehydrogenases.
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Substrates: The two-component system is implicated in redox signaling and cytochrome oxidase activity, in expression of the cell density-dependent gene ddcA and in bacterial colonization of plant surfaces. The RoxS/RoxR regulon includes genes involved in sugar and amino acid metabolism and the sulfur starvation response and elements of the respiratory chain (a cbb3 cytochrome oxidase, Fe-S clusters, and cytochrome c-related proteins) or genes participating in the maintenance of the redox balance. The RoxS/RoxR system controls a broad set of functions that have an influence on energy metabolism, such as formaldehyde and formate dehydrogenases.
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Substrates: significant number of genes are influenced directly or indirectly by the RoxSR two-component system. 173 genes are found showing reduced expression in EU58 (RoxSR mutant strain) in comparison to the wild type, whereas 84 genes are upregulated in the mutant
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Substrates: significant number of genes are influenced directly or indirectly by the RoxSR two-component system. 173 genes are found showing reduced expression in EU58 (RoxSR mutant strain) in comparison to the wild type, whereas 84 genes are upregulated in the mutant
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additional information
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Substrates: The two-component system is implicated in redox signaling and cytochrome oxidase activity, in expression of the cell density-dependent gene ddcA and in bacterial colonization of plant surfaces. The RoxS/RoxR regulon includes genes involved in sugar and amino acid metabolism and the sulfur starvation response and elements of the respiratory chain (a cbb3 cytochrome oxidase, Fe-S clusters, and cytochrome c-related proteins) or genes participating in the maintenance of the redox balance. The RoxS/RoxR system controls a broad set of functions that have an influence on energy metabolism, such as formaldehyde and formate dehydrogenases.
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additional information
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Substrates: significant number of genes are influenced directly or indirectly by the RoxSR two-component system. 173 genes are found showing reduced expression in EU58 (RoxSR mutant strain) in comparison to the wild type, whereas 84 genes are upregulated in the mutant
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Substrates: two-component regulatory system CopR/CopS is required for copper-inducible expression of the copper resistance operon
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Substrates: required for the activation of the C4-dicarboxylate transport structural gene dctA in free-living Rhizobium leguminosarum
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Substrates: the gene regulates transcription of the nifHDK operon and so limits the expression of nitrogen fixation activity to periods of low environmental concentrations of both oxygen and fixed nitrogen
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Substrates: role of the C-terminal domains in the photocycle of a light sensor histidine kinase Ppr having a photoactive yellow protein, PYP, domain as the photosensor domain, photocycles of the PYP domain of Ppr and of the full-length Ppr. The, overview
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Substrates: the two-component system regulates an osmosensing MAP kinase cascade
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Substrates: the two-component system regulates an osmosensing MAP kinase cascade
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Substrates: ompR-envZ is a two component regulatory system that plays an important role in the regulation of Vi polysaccharide synthesis in Salmonella typhi. One of the environmental signals for this regulation may be osmolarity
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Substrates: UhpB and perhaps UhpC play both positive and negative roles in the control of uhpT transcription
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Substrates: during bacterial chemotaxis, the binding of stimulatory ligands to chemoreceptors at the cell periphery leads to a response at the flagellar motor. Three proteins appear to be required for receptor-mediated control of swimming behavior, the products of the cheA, cheW, and cheY genes
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Substrates: during bacterial chemotaxis, the binding of stimulatory ligands to chemoreceptors at the cell periphery leads to a response at the flagellar motor. Three proteins appear to be required for receptor-mediated control of swimming behavior, the products of the cheA, cheW, and cheY genes
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Substrates: enzyme is required for the proper expression of the outer membrane proteins OmpC and OmpF
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Substrates: the two-component regulatory system phoP/phoQ controls Salmonella typhimurium virulence
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Substrates: the PhoP-PhoQ system exerts a master regulatory function for preventing bacterial overgrowth within fibroblasts
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Substrates: enzyme is involved in the regulation of expression of phosphoglycerate transport in Salmonella typhimurium. pgtB and pgtC genes are involved in the induction of the pgtP expression by modulating derepressor activity
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Substrates: PgtB and PgtC polypeptides modulate PgtA activity
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Substrates: enzyme is involved in regulation of the phosphate regulon
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Substrates: regulation of nitrogen fixation genes in Rhizobium meliloti is mediated by two proteins, FixL and FixJ, in response to oxygen availability, oxygen sensor
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Substrates: FixL senses an environmental signal and transduces it to FixJ, a transcriptional activator of nif and fix genes
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Substrates: genes dctB and dctD form a two-component system which responds to the presence of C4-dicarboxylates to regulate expression of a transport protein encoded by dctA
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Substrates: in free-living cells, the regulatory dctBD genes are absolutely required for the expression of the dctA gene
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Substrates: dctB-encoded protein includes a putative periplasmic N-terminal domain that senses the presence of dicarboxylates and a C-terminal cytoplasmic domain that activates the dctD-encoded protein
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Substrates: the ExoS-ChvI two-component regulatory system regulates succinoglycan production. ChvG is the sensor protein of the ChvG-ChvI two-component regulatory system
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Substrates: the ExoS-ChvI two-component regulatory system regulates succinoglycan production. ChvG is the sensor protein of the ChvG-ChvI two-component regulatory system
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Substrates: the two-component regulatory system afsQ1/afsQ2 is involved in secondary metabolism
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Substrates: the cutR-cutS operon regulates copper metabolism in Streptomyces
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Substrates: a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
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Substrates: a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
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Substrates: the SenS/SenR system of Streptomyces reticuli regulates the expression of the redox regulator FurS, the catalase-peroxidase CpeB and the heme-binding protein HbpS. SenS/SenR also participates in sensing redox changes, mediated by HbpS. The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner, presence of SenS/SenR leads to the synthesis of extracellular redox active proteins, overview
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Substrates: the SenS/SenR system of Streptomyces reticuli regulates the expression of the redox regulator FurS, the catalase-peroxidase CpeB and the heme-binding protein HbpS. SenS/SenR also participates in sensing redox changes, mediated by HbpS. The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner, presence of SenS/SenR leads to the synthesis of extracellular redox active proteins, overview
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Substrates: the enzyme is involved in chemical sensing
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Substrates: interaction of Hik2 with Rre1 and RppA, usage of recombinant N-terminally MBP-tagged proteins purified from Escherichia coli expression host
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Substrates: the enzyme is involved in chemotaxis
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Substrates: the enzyme is involved in regulation of density-dependent expression of luminescence in Vibrio harveyi
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Substrates: the enzyme is involved in regulation of density-dependent expression of luminescence in Vibrio harveyi
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Substrates: enzyme is involved in positive regulation of synthesis of extracellular enzymes and polysaccharide in Xanthomonas campestris pathovar campestris
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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Slr1759-Var I protein contains 0.11-0.26 mM cofactor per 1 mM protein
GDP
this kinase is uniquely specific for GTP in the forward and GDP in the reverse reaction. The G1 motif of BA2291 is highly modified from ATP specific histidine kinases, binding structure, modeling, overview
GTP
this kinase is uniquely specific for GTP in the forward and GDP in the reverse reaction. The G1 motif of BA2291 is highly modified from ATP specific histidine kinases, binding structure, modeling, overview
ATP
the ATP-binding domain of histidine kinases contains conserved motifs essential for autokinase activity. These include G1 and G2 boxes, which have the characteristic glycine signatures DxGxG and GxGxG, respectively
ATP
-
residue Ser492 resides on the ATP lid, near to the Mg2+ ion that coordinates the gamma-phosphate of ATP in the P4 active site
ATP
DesK displays a compact structure at the ATP-binding pocket: the ATP lid loop is short with no secondary structural organization and becomes ordered upon ATP loading. Sequence conservation mapping onto the molecular surface, semi-flexible protein-protein docking simulations, and structure-based point mutagenesis present a specific domain-domain geometry during autophosphorylation catalysis
flavin
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flavin-containing histidine kinase functions as a photoreceptor, the flavin chromophore, upon illumination, forms a cysteinyl-flavin adduct, which is the signaling state that activates the histidine kinase
flavin
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flavin-containing histidine kinase functions as a photoreceptor, the flavin chromophore, upon illumination, forms a cysteinyl-flavin adduct, which is the signaling state that activates the histidine kinase, regulates Brucella abortus virulence
heme
FixL is an oxygen-binding hemoprotein, the heme domain serves as the dioxygen switch in the FixL/FixJ two-component system
heme
the oxygen-detecting domain is a heme binding region that controls the activity of an attached histidine kinase. In the absence of bound ligand, the heme domain permits kinase activity. In the presence of bound ligand, this domain turns off kinase activity
heme
-
the Fe(II) heme-bound inactive form has kcat and Km(ATP) values of 0.0067/s and 0.078 mM, respectively, suggesting that its low activity reflects a low affinity for ATP relative to that of the Fe(III) form. The heme-free form exhibits low activity, with kcat and Km(ATP) values of 0.005/s and 0.0336 mM, respectively, suggesting that the heme iron complex is essential for high catalytic activity. The coordination and oxidation state of the sensor domain heme iron profoundly affect the enzyme's catalytic activity because they modulate its ATP binding affinity and thus change its kcat/Km(ATP) value
additional information
no activity with ATP, TTP, or CTP in autophosphorylation
-
additional information
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no activity with ATP, TTP, or CTP in autophosphorylation
-
additional information
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non-hydrolyzable ATP analogues (but not ATP or ADP) release P1 from the protein core (domains P3P4P5) and increase its mobility
-
additional information
LOV domains are blue-light sensory modules which bind a flavin molecule as cofactor. Activation of LOVHK by blue-light increases the autophosphorylation activity of the HK domain
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additional information
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LOV domains are blue-light sensory modules which bind a flavin molecule as cofactor. Activation of LOVHK by blue-light increases the autophosphorylation activity of the HK domain
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ag+
Cl-
activates, the signal input domain of Hik2 responds to environmental Cl- concentration, key for induction of activity
Cu+
0.14 molecules of Cu+ per enzyme molecule for the purified enzyme, and 0.23 molecules of Cu+ per enzyme molecule after dialysis against Ag+, Ni2+, Zn2+, and Cu+ ions
Cu2+
Fe
-
enzyme contains 2-labile 1-2 iron-sulphur [4Fe-4S]2+ clusters of the FNR-type
Fe2+
Fe3+
-
0.005 mM Fe3+ is able to enhance the phosphorylation level of SenS by a factor of 10 relative to the basal level
FeCl2
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enhances SenS autokinase activity in presence of HbpS, the activation is unaffected by DTT, but is enhanced by H2O2
FeCl3
-
enhances SenS autokinase activity strongly in presence of HbpS, H2O2 and DTT inhibit the activation
Mg2+
Zn2+
the sensor domain of CzcS senses the Zn(II) stimulus at micromole level in a tetrahedral geometry through its symmetry-related residues His55 and Asp60 on the dimer interface
additional information
Ag+
CusS forms a homodimer with four Ag(I) binding sites per dimeric complex, binding site structure, overview
Ag+
the periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize. No molecules of Ag+ per enzyme molecule for the purified enzyme, and 3.82 molecules of Ag+ per enzyme molecule after dialysis against Ag+, Ni2+, Zn2+, and Cu+ ions
Fe2+
-
the Fe(II) heme-bound inactive form has kcat and Km(ATP) values of 0.0067/s and 0.078 mM, respectively, suggesting that its low activity reflects a low affinity for ATP relative to that of the Fe(III) form. The heme-free form exhibits low activity, with kcat and Km(ATP) values of 0.005/s and 0.0336 mM, respectively, suggesting that the heme iron complex is essential for high catalytic activity
Fe2+
-
the presence of iron ions alone or in combination with H2O2 or dithiothreitol leads to significantly increased phosphorylation levels of SenS. 0.005 mM Fe2+ is able to enhance the phosphorylation level of SenS by a factor of 10 relative to the basal level, a combination of FeCl2 and H2O2 increases autophosphorylation activity by a factor of 20
Mg2+
-
required, activates CovR phosphorylation at high concentration. High-Mg2+ conditions increase phosphorylated CovR levels dependent on the presence of an intact CovS protein without influencing CovR production
additional information
addition of KCl, NaCl, and LiCl to M9 medium (pH 5.5) at final concentrations of 50 and 100 mM induces the transcriptional activity of ydeP but not addition of MgCl2
additional information
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addition of KCl, NaCl, and LiCl to M9 medium (pH 5.5) at final concentrations of 50 and 100 mM induces the transcriptional activity of ydeP but not addition of MgCl2
additional information
the structure of the periplasmic sensor domain of the histidine kinase CusS shows unusual metal ion coordination at the dimeric interface. Two symmetric metal binding sites are found at the dimeric interface, which are each formed by two histidines and one phenylalanine with an unusual cation-Pi interaction, the other metal ion binding sites are in a non-conserved region within each monomer. The metal ion binding site at the dimer interface is more important for function. Metal-induced dimerization results in increases in kinase activity in the cytoplasmic domains of CusS. Functional roles of the metal binding sites in CusS, overview
additional information
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the structure of the periplasmic sensor domain of the histidine kinase CusS shows unusual metal ion coordination at the dimeric interface. Two symmetric metal binding sites are found at the dimeric interface, which are each formed by two histidines and one phenylalanine with an unusual cation-Pi interaction, the other metal ion binding sites are in a non-conserved region within each monomer. The metal ion binding site at the dimer interface is more important for function. Metal-induced dimerization results in increases in kinase activity in the cytoplasmic domains of CusS. Functional roles of the metal binding sites in CusS, overview
additional information
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the autokinase activity of SenS is not affeted by Zn2+, H2O2, and DTT
additional information
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the combination of 5 mM dithiothreitol and 0.005 mM FeCl2, or 5 mM dithiothreitol and 0.005 mM FeCl3, or 0.005 mM FeCl3 and 5 mM H2O2 has no effect on phosphorylation level of SenS, H2O2 prevents the activation by Fe3+
additional information
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ZnCl2 is not able to change the autokinase activity of SenS
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3-decanoyl-4,5,7-trihydroxynaphthalen-2-yl)acetic acid
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IC50 of 0.0095 mg/ml
(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)methanaminium chloride
2-(3,4-dimethoxyphenyl)-N-[(5-phenylfuran-2-yl)methyl]ethanaminium
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2-(4-[2-[4-(4-chlorobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
2-(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
2-[[(4-amino-1,2,5-oxadiazol-3-yl)carbonyl]amino]-N-[4-(thiophen-2-ylmethoxy)benzyl]ethanaminium
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2-[[(4-amino-1,2,5-oxadiazol-3-yl)carbonyl]amino]-N-[[5-(3-chloro-4-methoxyphenyl)furan-2-yl]methyl]ethanaminium
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3,6-diamino-5-cyano-4-phenyl-thieno[2,3-b]pyridine-2-carboxylic acid (4-bromo-phenyl)amide
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competitive inhibitor of the coupled reaction of histidine kinase HpkA HK and the cognate response regulator DrrA RR
6-(2,6-dimethylmorpholin-4-yl)-9H-purine
lead compound for inhibitor development
7-(4-fluorophenyl)-6-(pyridin-4-yl)-5H-pyrrolo[2,3-b]pyrazine
compound is able to displace ADP-BODIPY from the HK853 ATP-binding domain and inhibits HK853 and Streptococcus pneumoniaeVicK activity at non-aggregating concentrations. Compound may only poorly penetrate the bacterial envelope or lacks sufficient potency to yield measurable effects
cyanide
-
autokinase activity of the purified ethylene resistant 1 is completely abolished by 2 mM cyanide
ethylene
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autokinase activity of the purified ethylene resistant 1 is completely abolished by 2 mM ethylene
Fe(II)-CO complex
-
the Fe(II)-CO complex of the heme nitric oxide/oxygen protein inhibits the autophosphorylation of the operon-associated histidine kinase
Fe(II)-NO complex
-
the Fe(II)-NO complex of the heme nitric oxide/oxygen protein inhibits the autophosphorylation of the operon-associated histidine kinase, whereas the ligand-free heme nitric oxide/oxygen protein has no effect on the kinase
HCl
-
cytoplasmic phosphorylated AtoS is sensitive to treatment with 1 N HCl but stable in the presence of 1 N NaOH
heme-binding protein HbpS
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inhibits autophosphorylation activity of the enzyme in absence of redox reagents and hemin, but activates slightly in presence of hemin and strongly in presence of FeCl2 and FeCl3, DTT increases the activation with FeCl2, but inhibits activation with FeCl3, while H2O2 strongly increases the activation by FeCl2 and completely inhibits activation with FeCl3, overview
-
kinase inhibitor protein
-
the kinase inhibitor protein KipI prevents sporulation by binding KinA and inhibiting the autophosphorylation reaction
-
N,N-dipropyl-9H-purin-6-amine
lead compound for inhibitor development
N-(2-phenylethyl)-9H-purin-6-amine
lead compound for inhibitor development
N-(3,3,5-trimethylcyclohexyl)-9H-purin-6-amine
lead compound for inhibitor development
N-phenyl-9H-purin-6-amine
does not aggregate HK853 even at above 1.25 mM
N-[[5-(2-fluorophenyl)furan-2-yl]methyl]-3-[(1-methyl-1H-tetrazol-5-yl)sulfanyl]propan-1-aminium
-
N-[[5-(3-chloro-4-fluorophenyl)furan-2-yl]methyl]-3-[(1-methyl-1H-tetrazol-5-yl)sulfanyl]propan-1-aminium
-
Na+
strongly inhibits the autophosphorylation activity of Hik2. 0.5 M NaCl reduces the organism's growth rate by 50%
NaCl
increased NaCl concentrations convert the active hexamer into an inactive tetramer. The action of NaCl appears to be confined to the Hik2 kinase domain
suppressor of dnaA
-
Sda, inhibits KinA by directly binding to the autokinase domain
-
YycH
an extracytoplasmic membrane anchored protein. Enzyme YycG activity in non-dividing cells is suppressed by its interaction with YycH and YycI. YycG regulation is accomplished through its transmembrane and extra-membrane domains interacting with the membrane associated YycH and YycI proteins that do not localize to the divisome
-
YycI
an extracytoplasmic membrane anchored protein. Enzyme YycG activity in non-dividing cells is suppressed by its interaction with YycH and YycI. YycG regulation is accomplished through its transmembrane and extra-membrane domains interacting with the membrane associated YycH and YycI proteins that do not localize to the divisome
-
(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)methanaminium chloride
-
-
(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)methanaminium chloride
-
-
(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)methanaminium chloride
-
-
(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)methanaminium chloride
-
-
2-(4-[2-[4-(4-chlorobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
-
-
2-(4-[2-[4-(4-chlorobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
-
-
2-(4-[2-[4-(4-chlorobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
-
-
2-(4-[2-[4-(4-chlorobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
-
-
2-(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
-
-
2-(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
-
-
2-(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
-
-
2-(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
-
-
Cu2+
the wild-type strain experiences copper susceptibility at 2.75 mM CuSO4, whereas DELTAcusS mutant cells show a phenotype at lower concentrations
Mg2+
-
PhoQ is strongly repressed in divalent cation-replete medium at 10 mM Mg2+
Mg2+
-
PhoQ is strongly repressed in divalent cation-replete medium at 10 mM Mg2+
Sda
-
potent inhibitor of KinB autophosphorylation, Sda directly inhibits sporulation histidine kinase in response to DNA damage and replication defects, Sda acts to sterically block communication between the catalytic ATP-binding and dimerization/histidinephosphotransfer domains required for autophosphorylation, as well as to sterically block communication between the response regulator Spo0F and DHp domain required for phosphotransfer and phosphatase activities
-
Zn2+
Zn2+ binding negatively regulates the WalKR regulon. Zn2+ binding directly influences the relative positioning of the PAS and catalytic domains of WalK
additional information
the virulence plasmid-encoded sensor domains of BA2291 have a regulatory effect in vivo on the activity of full-length BA2291, by converting it from a normally functional sporulation kinase to an enzyme that inhibits sporulation, molecular mechanism
-
additional information
-
the virulence plasmid-encoded sensor domains of BA2291 have a regulatory effect in vivo on the activity of full-length BA2291, by converting it from a normally functional sporulation kinase to an enzyme that inhibits sporulation, molecular mechanism
-
additional information
-
in the dark, roughly an order of magnitude fewer bacteria survive, a survival rate no better than that of the LOV-HK knockout mutant
-
additional information
-
thermal transition of HK1 is a two-state process and that of HK2 is a three-state process. Urea denaturation of HK1 and HK2 is a three-state and two-state process, respectively
-
additional information
-
YycH and YycI are two auxiliary membrane proteins that inhibit the activity of YycG HK in Bacillus subtilis. Both YycH and YycI are required to inhibit the dimerization of YycG
-
additional information
YycH and YycI are two auxiliary membrane proteins that inhibit the activity of YycG HK in Bacillus subtilis. Both YycH and YycI are required to inhibit the dimerization of YycG
-
additional information
upon salt and/or hyperosmotic signal, the activity of Hik2 is inhibited. KCl does not inhibit the autophosphorylation activity of Hik2
-
additional information
not inhibitory at 1.25 mM: idelalisib, ibrutinib; structure-activity relationship assessment of adenine-based inhibitors using biochemical and docking methods. Interaction of an inhibitor's amine group with the conserved active-site Asp is essential for activity and likely dictates its orientation in the binding pocket. A N-NH-N triad in the inhibitor scaffold is highly preferred for binding to conserved Gly:Asp:Asn residues. Hydrophobic electron-withdrawing groups at several positions in the adenine core enhance potency. Groups that target the ATP-lid portion of the catalytic domain, such as a six-membered ring, confer selectivity for histidine kinases
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-dimethoxyphenol
-
activation of VirA increases in the absence of enzyme aas 285-293
alanine
-
stimulates, stimulation pattern of MtrA is similar to that of MtrB
auto-inducible protein I
-
dose-dependent activation by autoinducing peptide
-
betaine
-
stimulates, stimulation pattern of MtrA is similar to that of MtrB
ethanolamine
-
induces a 15fold increase in the rate of autophosphorylation in vitro of the HK17 sensor histidine kinase
fructose
-
stimulates, stimulation pattern of MtrA is similar to that of MtrB
glucose
-
stimulates, stimulation pattern of MtrA is similar to that of MtrB
glutamate
-
stimulates, stimulation pattern of MtrA is similar to that of MtrB
heme-binding protein HbpS
-
inhibits autophosphorylation activity of the enzyme in absence of redox reagents and hemin, but activates slightly in presence of hemin and strongly in presence of FeCl2 and FeCl3, DTT increases the activation with FeCl2, but inhibits activation with FeCl3, while H2O2 strongly increases the activation by FeCl2 and completely inhibits activation with FeCl3, overview
-
L-glutamate
-
stimulates, more efficient stimulation of MtrB than MtrA
lysine
-
stimulates, stimulation pattern of MtrA is similar to that of MtrB
maltoheptaose
-
stimulates, stimulation pattern of MtrA is similar to that of MtrB
maltose
-
stimulates, stimulation pattern of MtrA is similar to that of MtrB
maltotriose
-
stimulates, stimulation pattern of MtrA is similar to that of MtrB
mucin
the enzyme ChiS is activated 7.4fold in presence of intestinal mucin in vivo and in media supplemented with 2% w/v porcine mucin, the isogenic chiS mutant (ChiS?) shows less growth compared to the wild-type strain ChiS+ in the presence of mucin supplemented media. Activation of ChiS in the host intestine
-
proline
-
stimulates, stimulation pattern of MtrA is similar to that of MtrB
Ssl3451 protein
-
enhances the autophosphorylation activity of the histidine kinase Hik33 by associating with it with a 1:1 stoichiometry both in vitro and in vivo, but does not affect its dephosphorylation
-
subtilin
subtilin activates the two-component system SpaRK of Bacillus subtilis to autoinduce its biosynthesis. Amino acid position 20 is crucial for SpaK activation by subtilin. An engineered nisin molecule with phenylalanine at position 20 (nisin N20F) is able to activate SpaK in a specific manner. In combination with the N-terminal tryptophan of subtilin (nisin I1W/N20F), SpaK autoinduction reaches almost the level of subtilin-mediated autoinduction. The overall structure of subtilin is also important for its association with the histidine kinase. The destruction of the second lanthionine ring (subtilin C11A, ring B), as well as mutations that interfere with the flexibility of the hinge region located between lanthionine rings C and D (subtilin L21P/Q22P), abolish SpaK autoinduction. The C-terminal part of subtilin is needed for efficient SpaK autoinduction, but the destruction of lanthionine rings D and E has no measurable impact
-
sucrose
-
stimulates, stimulation pattern of MtrA is similar to that of MtrB
trehalose
-
stimulates, stimulation pattern of MtrA is similar to that of MtrB
UhpC
-
UhpC stimulates UhpB autophosphorylation in the presence of D-glucose 6-phosphate
-
additional information
-
small molecule inducers (phenols and sugars) are produced at a wound site and activate the enzyme to induce gene transfer processes, VirA serves as the histidine autokinase antenna that phosphorylates VirG as the active transcriptional regulator
-
additional information
the virulence plasmid-encoded sensor domains of BA2291 have a regulatory effect in vivo on the activity of full-length BA2291, by converting it from a normally functional sporulation kinase to an enzyme that inhibits sporulation, molecular mechanism
-
additional information
-
the virulence plasmid-encoded sensor domains of BA2291 have a regulatory effect in vivo on the activity of full-length BA2291, by converting it from a normally functional sporulation kinase to an enzyme that inhibits sporulation, molecular mechanism
-
additional information
-
KinC becomes active by forming a homotetramer via the N-terminal PAS domain, but its activity is independent of both the lipid raft and the potassium leakage
-
additional information
exposure to light increases the autophosphorylation activity of the enzyme
-
additional information
-
exposure to light increases the autophosphorylation activity of the enzyme
-
additional information
-
light-activated, 2fold increase in transcription of the LOV-HK gene at a pH similar to that within infected macrophages
-
additional information
-
liposome shrinkage is not necessary for MtrB activation, MtrB is activated upon the addition of various chemical compounds, like sugars, amino acids, and polyethylene glycols, these may act via a change of the hydration state of the protein shifting MtrB into the active state, for activation it is essential that solutes are added at the same side as the cytoplasmic domains of the kinase are located
-
additional information
a high concentration of alkali metals (Na+, K+) in addition to low pH is essential for the activation of histidine kinase EvgS. EvgS/EvgA is activated under mildly acidic conditions at pH 5.0-5.5. EvgS has a large periplasmic sensor region consisting of two tandem bacterial periplasmic solute-binding protein (PBPb) domains at its N-terminus. The periplasmic sensor region of EvgS is necessary for EvgS activation, and Leu152, located within the first PBPb domain, is involved in the activation. Alkali metals are perceived at the periplasmic sensor region, whereas the cytoplasmic linker domain, connecting the transmembrane region and the histidine kinase domain, is required for low-pH perception
-
additional information
-
a high concentration of alkali metals (Na+, K+) in addition to low pH is essential for the activation of histidine kinase EvgS. EvgS/EvgA is activated under mildly acidic conditions at pH 5.0-5.5. EvgS has a large periplasmic sensor region consisting of two tandem bacterial periplasmic solute-binding protein (PBPb) domains at its N-terminus. The periplasmic sensor region of EvgS is necessary for EvgS activation, and Leu152, located within the first PBPb domain, is involved in the activation. Alkali metals are perceived at the periplasmic sensor region, whereas the cytoplasmic linker domain, connecting the transmembrane region and the histidine kinase domain, is required for low-pH perception
-
additional information
a sequential kinase activation model may involve helical bending of the DHp domain and repositioning of the CA domains. Model of VicK autokinase activation, overview
-
additional information
-
hemin-treated HbpS enhances SenS autophosphorylation by 30fold under redox conditions using either H2O2 or dithiothreitol
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
autophosphorylation reaction kinetics, overview. Km values in autophosphorylation of the heme Fe(III)-OH(-), Fe(III)-cyanide, Fe(III)-imidazole, and Fe(II)-O2 bound active AfGcHK forms are 0.0189-00.0354 mM
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
kinase activity of recombinant enzyme AgrCTM5-6C in N,N-dimethyldodecylamine N-oxide micelles or proteoliposomes
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kcat values in autophosphorylation of the heme Fe(III)-OH(-), Fe(III)-cyanide, Fe(III)-imidazole, and Fe(II)-O2 bound active AfGcHK forms are 0.0183-0.02/s
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00062
3,6-diamino-5-cyano-4-phenyl-thieno[2,3-b]pyridine-2-carboxylic acid (4-bromo-phenyl)amide
-
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.126
2-chloro-9-D-ribofuranosyl-9H-purin-6-amine
Thermotoga maritima
23°C, pH not specified in the publication
0.095
2-chloro-9-methyl-9H-purin-6-amine
Thermotoga maritima
23°C, pH not specified in the publication
0.156
2-chloro-9H-purin-6-amine
Thermotoga maritima
23°C, pH not specified in the publication
0.0953
6-(2,6-dimethylmorpholin-4-yl)-9H-purine
Thermotoga maritima
23°C, pH not specified in the publication
0.118
6-chloro-9-D-ribofuranosyl-9H-purin-2-amine
Thermotoga maritima
23°C, pH not specified in the publication
0.0237
7-(4-fluorophenyl)-6-(pyridin-4-yl)-5H-pyrrolo[2,3-b]pyrazine
Thermotoga maritima
pH not specified in the publication, temperature not specified in the publication
0.0496
N,N-dipropyl-9H-purin-6-amine
Thermotoga maritima
23°C, pH not specified in the publication
0.145
N-(2-phenylethyl)-9H-purin-6-amine
Thermotoga maritima
23°C, pH not specified in the publication
0.131
N-(3,3,5-trimethylcyclohexyl)-9H-purin-6-amine
Thermotoga maritima
23°C, pH not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.04
wild-type strain in absence of mucin, 37°C, pH not specified in the publication
0.1805
wild-type strain in presence of mucin, 37°C, pH not specified in the publication
additional information
-
activities of wild-type and truncated mutant SenS under different conditions, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.4 - 8.1
-
the light/dark difference spectra of Ppr-PYP are pH sensitive, pH-dependent equilibrium change between Ppr-PYPL and Ppr-PYPM, overview
additional information
additional information
mechanism for the pH-dependent conformational change of the extracellular sensor domain of the DraK protein involving residues E83, E105, and E107 with very high pKa values, overview
additional information
-
mechanism for the pH-dependent conformational change of the extracellular sensor domain of the DraK protein involving residues E83, E105, and E107 with very high pKa values, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Agrobacterium tumefaciens C58 / ATCC 33970
19 different isolates, gene AlHK1
UniProt
brenda
gene BA2291, the organism contains nine genes encoding putative sporulation histidine kinases
UniProt
brenda
all strains derived from Brucella abortus 544 NalR, XDB1104 strain
-
-
brenda
-
Q892E7, Q893B1, Q893C2, Q893H6, Q893K0, Q893l4, Q893S8, Q894l7, Q894P4, Q894W4, Q895Y4, Q896X1, Q897D4, Q897U6, Q898N3, Q899I6, Q899l3
SwissProt
brenda
-
SwissProt
brenda
-
SwissProt
brenda
differs from strain NCTC8325 and contains a number of genetic polymorphisms
-
-
brenda
belongs to the group B streptococci, strains A909 and COH1 are clinical isolates belonging to capsular polysaccharide serotype 1a and serotype III, respectively
A0A8G2N576
UniProt
brenda
gene BA2291, the organism contains nine genes encoding putative sporulation histidine kinases
UniProt
brenda
-
SwissProt
brenda
wild-type strain JH642 and conditional ftsZ expression strain KP444, gene yycG
SwissProt
brenda
all strains derived from Brucella abortus 544 NalR, XDB1104 strain
-
-
brenda
-
Q8YBU4, Q8YC53, Q8YDX2, Q8YE43, Q8YE51, Q8YER2, Q8YF74, Q8YF98, Q8YFB6, Q8YFD9, Q8YG26, Q8YG34, Q8YG37, Q8YH57, Q8YHD4, Q8YHD6, Q8YIF2, Q8YIR9
SwissProt
brenda
-
SwissProt
brenda
-
P07363, P08400, P0AEC3, P0AEC7, P0AEJ4, P0DMC5, P18392, P21865, P23837, P27896, P30847, P30855, P39453, P40719, P77485, P77510, Q06067
SwissProt
brenda
O6
A0A0H2V5G6, A0A0H2V5U0, A0A0H2V5U2, A0A0H2V759, A0A0H2V7C4, A0A0H2V7H2, A0A0H2V832, A0A0H2V920, A0A0H2V999, A0A0H2VA69, A0A0H2VAX5, A0A0H2VBC5, A0A0H2VBI7, A0A0H2VBT9, A0A0H2VCD4, A0A0H2VD14, A0A0H2VD53, A0A0H2VD68, A0A0H2VDZ7, A0A0H2VFL1
UniProt
brenda
sensor protein, the two components are encoded by PP_0887 (roxS, sensor protein) and PP_0888 (roxR, response regulator) which are transcribed in a single unit.
UniProt
brenda
sensor protein, the two components are encoded by PP_0887 (roxS, sensor protein) and PP_0888 (roxR, response regulator) which are transcribed in a single unit.
UniProt
brenda
-
SwissProt
brenda
-
SwissProt
brenda
-
P08982, P09384, P0A2D9, P0DM80, P27668, P36557, P37433, P37461, P58662, Q8XG60, Q8ZJU5, Q8ZKD8, Q8ZKZ3, Q8ZLR5, Q8ZLZ9, Q8ZMM5, Q8ZN78, Q8ZP35, Q8ZPL6, Q8ZPP5, Q8ZPP6, Q8ZQ54, Q8ZQW4, Q8ZR59, Q8ZRE1, Q9L9E4
SwissProt
brenda
differs from strain NCTC8325 and contains a number of genetic polymorphisms
-
-
brenda
strain ATCC BAA-255/R6
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
optimal growth temperature for Synechocystis is 32-38°C, for both wild-type and DELTAHik34 mutant strains showing the same growth rates
brenda
expressed in geranium florets long before they are receptive to pollination and transcript levels remain constant throughout floral development
brenda
the level of expression of PE-ETR1 does not significantly change over the course of ripening, however, the mRNA levels of PE-ETR1 is much higher in arils than in seeds
brenda
LeETR2 mRNA expression is down-regulated in senescing leaf petioles
brenda
-
RodK is present in vegetative cells and remains present until the late aggregation stage, after which the level decreases in a manner that depends on the intracellular A-signal
brenda
additional information
-
histidine kinases of the organism show temporally and spatially different expression during the life cycle, e.g. expression of HK genes during sexual and asexual development, overview
brenda
-
histidine kinases of the organism show temporally and spatially different expression during the life cycle, e.g. expression of HK genes during sexual and asexual development, overview
-
brenda
-
HK1 is a receptor component with spatially restricted expression in the syncytial endosperm where endosperm transfer cells emerge
brenda
LeETR2 mRNA is expressed at low levels throughout the plant but is induced in imbibing seeds prior to germination
brenda
LeETR2 mRNA expression is down-regulated in elongating seedlings
brenda
additional information
-
spatial distribution of endoplasmic reticulum-localized CKI1 in the syncytial embryo sac is mediated by nuclear position and migration, overview
brenda
additional information
no expression of CKI1 in seedling, roots, stem, and leaves
brenda
additional information
-
no expression of CKI1 in seedling, roots, stem, and leaves
-
brenda
additional information
-
spatial distribution of endoplasmic reticulum-localized CKI1 in the syncytial embryo sac is mediated by nuclear position and migration, overview
-
brenda
additional information
FrzE is clearly present during vegetative growth and at much lower levels during development
brenda
additional information
EspA developmental expression pattern, mutational analysis, overview
brenda
additional information
-
EspA developmental expression pattern, mutational analysis, overview
brenda
additional information
LeETR1 is expressed constitutively in all plant tissues examined
brenda
additional information
LeETR1 is expressed constitutively in all plant tissues examined
brenda
additional information
-
LeETR1 is expressed constitutively in all plant tissues examined
brenda
additional information
mRNA is constitutively expressed in vegetative and reproductive tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the multidomain protein DcuS possesses functional domains in the periplasm, within the membrane and in the cytoplasm, the localization depends on the functional state, overview
-
brenda
additional information
-
KinC localizes as puncta along the cell membrane in a manner independent of FloTA proteins, localization pattern of GFP-tagged KinC, overview. KinC does not localize at specific sites on membrane under the conditions tested
-
brenda
-
KinC localizes as puncta along the cell membrane in a manner independent of FloTA proteins, localization pattern of GFP-tagged KinC, overview. KinC does not localize at specific sites on membrane under the conditions tested
-
-
brenda
division septum, a cytoplasmic domain of YycG is sufficient for septum localization. All recombinant truncated YycG constructs including the shortest one that featured only the cytoplasmic PAS and the two catalytic HisKA and HATPase domains retain the ability to localize to the septum
brenda
-
division septum, a cytoplasmic domain of YycG is sufficient for septum localization. All recombinant truncated YycG constructs including the shortest one that featured only the cytoplasmic PAS and the two catalytic HisKA and HATPase domains retain the ability to localize to the septum
-
brenda
the hybrid histidine kinase is localized in both the cytoplasm and the plasma membrane
brenda
-
the hybrid histidine kinase is localized in both the cytoplasm and the plasma membrane
-
brenda
-
is localized at the old pole of the large cell, after division and growth, the small cell acquires PdhS at its old pole, polar localization of PdhS is maintained during a cellular infection by bovine macrophages
brenda
-
is localized at the old pole of the large cell, after division and growth, the small cell acquires PdhS at its old pole, polar localization of PdhS is maintained during a cellular infection by bovine macrophages
-
brenda
-
RodK is a soluble cytoplasmic protein, which contains an N-terminal sensor domain, a histidine protein kinase domain and three receiver domains
brenda
enzyme is anchored to the cytoplasmic membrane by the amino-terminal region
-
brenda
structure-function relationship in the cytoplasmic PAS domain, the multidomain protein DcuS possesses functional domains in the periplasm, within the membrane and in the cytoplasm, the localization depends on the functional state, overview
brenda
ETR1 of Arabidopsis contains transmembrane domains responsible for ethylene binding and membrane localization
brenda
-
a transmembrane protein with a periplasmic domain
-
brenda
-
a transmembrane protein with a periplasmic domain
-
-
brenda
-
the enzyme is distributed evenly about the membrane of Escherichia coli
-
brenda
-
EnvZ with a N-terminal cytoplasmic tail (residues 1-15), two transmembrane domains (residues 16-34 and residues 163-179) flanking a periplasmic domain (residues 48-162), and a cytoplasmic domain (residues 180-450). The cytoplasmic domain can be further dissected into a linker or HAMP domain (residues 180-222), domain A (dimerization and histidine containing domain, residues 223-289) and domain B (catalysis assisting and ATP binding domain, residues 290-450), UhpB contains eight transmembrane segments
-
brenda
-
bound, PilS is retained to the poles of Pseudomonas aeruginosa
-
brenda
NtrY is likely to represent the transmembrane sensor protein element in the two-component regulatory system
brenda
the enzyme structure displays an N-terminal sensor domain (about 150 residues) with almost no extracellular region, other than the loops that connect the four or five transmembrane segments
brenda
the YycG kinase is associated in the membrane as a complex with YycH and YycI through interaction of their transmembrane domains
brenda
-
the enzyme structure displays an N-terminal sensor domain (about 150 residues) with almost no extracellular region, other than the loops that connect the four or five transmembrane segments
-
brenda
-
the YycG kinase is associated in the membrane as a complex with YycH and YycI through interaction of their transmembrane domains
-
brenda
transmembrane regions of EnvZ play roles in transmembrane signaling
brenda
EnvZ is a transmembrane protein with histidine kinase activity in its cytoplasmic region. The cytoplasmic region contains two functional domains: domain A, residues 223-289, contains the conserved histidine residue H243, a site of autophosphorylation as well as transphosphorylation to the conserved D55 residue of response regulator OmpR
brenda
a large periplasmic domain is lacking and an extended cytoplasmic domain is present besides the kinase domain
brenda
the region between the hydrophobic segments of CpxA is periplasmic, whereas the region carboxy-terminal to the second such segment is cytoplasmic. CpxA functions as a trans-membrane sensory protein
brenda
DcuS contains two putative transmembrane helices flanking an approximately 140-residue N-terminal domain apparently located in the periplasm
brenda
DcuS is a membrane-integral sensor kinase, and the sensory and kinase domains are located on opposite sides of the cytoplasmic membrane
brenda
membrane-bound protein comprising at least three cytoplasmic domains
brenda
KdpD is anchored to the membrane by four membrane-spanning segments near its middle, with both C-terminal and N-terminal portions in the cytoplasm
brenda
KdpD has four membrane-spanning segments in the middle of the polypeptide chain, whereas N and C terminus are both cytoplasmic
brenda
-
membrane-integral protein, DcuS and CitA accumulate at the cell poles
brenda
CusS is a membrane-associated histidine kinase with a periplasmic sensor domain connected to the cytoplasmic ATP-binding and catalytic domains through two transmembrane helices
brenda
a periplasmic sensor domain is flanked by transmembrane alpha-helices which link it to conserved cytoplasmic catalytic domains
brenda
CitA represents a membrane-bound sensor kinase consisting of a periplasmic domain flanked by two transmembrane helices, a linker domain and the conserved kinase or transmitter domain
brenda
CitA contains in the N-terminal half, two putative transmembrane helices which enclosed a presumably periplasmic domain of about 130 amino acids
brenda
N-terminal region may be located in the periplasm and its C-terminal region in the cytoplasm
brenda
membrane-bound sensor-kinase with two potential membrane-spanning sequences in the N-terminal region
brenda
associated with
brenda
EnvZ contained two hydrophobic stretches typical of transmembrane regions
brenda
FixL has features of a transmembrane protein
brenda
FixL is a membrane protein containing four possible transmembrane segments
brenda
dctB-encoded protein includes a putative periplasmic N-terminal domain that senses the presence of dicarboxylates and a C-terminal cytoplasmic domain that activates the dctD-encoded protein
brenda
-
an integral membrane protein, protein transmembrane topology in proteoliposomes is determined using membrane-impermeable and membrane-permeable thiol-reactive reagents, overview
brenda
-
Hik33 perceives the cold signal via rigidification of membrane lipids
brenda
the hybrid histidine kinase is localized in both the cytoplasm and the plasma membrane
brenda
-
the hybrid histidine kinase is localized in both the cytoplasm and the plasma membrane
-
brenda
the multidomain protein DcuS possesses functional domains in the periplasm, within the membrane and in the cytoplasm, the localization depends on the functional state, overview
brenda
VicK has one transmembrane domain, amino acids 9-30, that anchors itself to the cytoplasmic membrane
brenda
-
VicK has one transmembrane domain, amino acids 9-30, that anchors itself to the cytoplasmic membrane
-
brenda
additional information
-
no signal peptide or transmembrane region is predicted
-
brenda
additional information
the enzyme lacks transmembrane domains
-
brenda
additional information
-
the enzyme lacks transmembrane domains
-
brenda
additional information
-
the enzyme lacks transmembrane domains
-
-
brenda
additional information
YycG is located at the division septum in growing cells, YycG localization is dependent upon FtsZ, but independent of YycH and YycI
-
brenda
additional information
-
YycG is located at the division septum in growing cells, YycG localization is dependent upon FtsZ, but independent of YycH and YycI
-
brenda
additional information
the enzyme has a C-terminal cytoplasmic catalytic core of about 220 residues
-
brenda
additional information
-
the enzyme has a C-terminal cytoplasmic catalytic core of about 220 residues
-
brenda
additional information
-
the enzyme has a C-terminal cytoplasmic catalytic core of about 220 residues
-
-
brenda
additional information
the structure of the periplasmic sensor domain of the histidine kinase CusS shows unusual metal ion coordination at the dimeric interface
-
brenda
additional information
-
the structure of the periplasmic sensor domain of the histidine kinase CusS shows unusual metal ion coordination at the dimeric interface
-
brenda
additional information
the signal input domain of Hik2 does not contain any membrane-spanning regions except the GAF domain, so it is expected to be a cytosolic protein
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brenda
additional information
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the signal input domain of Hik2 does not contain any membrane-spanning regions except the GAF domain, so it is expected to be a cytosolic protein
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brenda
additional information
Vibrio cholerae serotype O1 MO45
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periplasmic sensor domains
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brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the CusS histidine kinase has overall sequence identity to putative metal-sensing HKs such as SilS (56%), CopS (42%), PcoS (38%) and CinS (35%)
evolution
glycerol and manganese have a similar biofilm-promoting effect in two related Bacillus species, Bacillus licheniformis and Bacillus cereus, indicating that the biofilm-promoting effect of GM is conserved in Bacillus species
evolution
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CheA differs from sensor histidine kinases in several ways: CheA does not contain a transmembrane domain, relying instead on P5 and CheW for interaction with transmembrane components. It has the phosphorylatable His residue on a separate domain (P1) instead of the dimerization domain (P3), and it utilizes a separate docking domain (P2) for CheY. P2 is not necessary for phosphotransfer to the response regulator CheY per se but variants lacking the P2 domain (DELTAP2) exhibit a reduced phosphotransfer rate relative to full-length CheA (CheAFL) and support a lower extent of chemotaxis. The linkers between the CheA domains play important roles in CheA activity
evolution
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the Brucella histidine kinase domain belongs to the HWE histidine kinase family. The HWE HK domains are present in LOV-HKs and bacteriophytochromes among other proteins
evolution
histidine kinase Shk1 is a member of the histidine kinase class III, whose members are all known to signal through the high-osmolarity glycerol mitogen-activated protein kinase
evolution
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the Arabidopsis thaliana genome encodes eight canonical HKs (AHK1-5, ETR1, ERS1, and CKI1), five canonical AHPs (AHP1-5), and one pseudo-AHP (AHP6) that carries an asparagine instead of the critical histidine residue
evolution
different structures of FimS kinase domains in strains strain ATCC 33277 and strain W83
evolution
different structures of FimS kinase domains in strains strain ATCC 33277 and strain W83. Although the production of FimR in W83 is modest, the protein still is detectable and can be functional because its amino acid sequence is almost identical to that of strain ATCC 33277, except for the alteration of one residue from serine to threonine, S209T
evolution
the class I enzyme DesK belongs to the HK family HPK7, which includes the nitrogen metabolism regulators NarX/Q and the antibiotic sensor LiaS among other important sensor kinases
evolution
while the GacS/GacA two-component system is widely distributed throughout the bacterial kingdom, the molecular switch formed by the hybrid LadS, PA1611 and RetS histifine kinases is unique to the Pseudomonas species, though it can function in very different ways in phylogenetically related Pseudomonas species
evolution
Brucella spp. genomes encode a LOV-domain-containing protein that is associated to a PAS (Per, Arnt and Sim) domain plus a HK domain (LOVHK), which belongs to the HWE family
evolution
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glycerol and manganese have a similar biofilm-promoting effect in two related Bacillus species, Bacillus licheniformis and Bacillus cereus, indicating that the biofilm-promoting effect of GM is conserved in Bacillus species
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evolution
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the class I enzyme DesK belongs to the HK family HPK7, which includes the nitrogen metabolism regulators NarX/Q and the antibiotic sensor LiaS among other important sensor kinases
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evolution
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Brucella spp. genomes encode a LOV-domain-containing protein that is associated to a PAS (Per, Arnt and Sim) domain plus a HK domain (LOVHK), which belongs to the HWE family
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evolution
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different structures of FimS kinase domains in strains strain ATCC 33277 and strain W83
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evolution
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different structures of FimS kinase domains in strains strain ATCC 33277 and strain W83. Although the production of FimR in W83 is modest, the protein still is detectable and can be functional because its amino acid sequence is almost identical to that of strain ATCC 33277, except for the alteration of one residue from serine to threonine, S209T
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evolution
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histidine kinase Shk1 is a member of the histidine kinase class III, whose members are all known to signal through the high-osmolarity glycerol mitogen-activated protein kinase
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malfunction
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HP0244 deletion abolishes urease activation and assembly, impairs cytoplasmic and periplasmic pH homeostasis, and depolarizes the cells, with an about 7-log loss of survival at pH 2.5, even in 10 mM urea
malfunction
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genetic modifications of cytokinin-independent1 activity in Arabidopsis cause dysfunction of the two-component signaling pathway and defects in procambial cell maintenance, loss-of-function histidine kinase2 and histidine kinase3 mutants show defects in procambium proliferation and an absence of secondary growth
malfunction
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Arabidopsis mutants lacking HK5 show reduced stomatal closure in response to H2O2, overexpression of HK5 results in constitutively less stomatal closure
malfunction
the wild-type strain experiences copper susceptibility at 2.75 mM CuSO4, whereas DELTAcusS mutant cells show a phenotype at lower concentrations. The growth defects observed in the DELTAcusS strain can be partially rescued by expression of intact CusS from a plasmid
malfunction
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residue 293 plays a central role in the altered structural specificity of the DELTA280-293 truncation, activation of VirA by phenols increases in the absence of enzyme aas 285-293. Mutations in the L domain can rescue null mutants in the R domain. Y293F substitution switches VirA from requiring two separate inputs to an OR gate, responding to both signals separately
malfunction
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ectopic CKI1 expression generates non-propagating seeds with dual fertilized endosperms and no embryos. CKI1 loss-of-function mutants exhibit gametophytic defects resulting in semi-sterility. Cell specification is defective in cki1 mutant embryo sacs. Autonomous endosperms arise from ectopic central cells in the PRC2 fis2 (fertilization independent 2) mutant
malfunction
A0A8G2N576
group B streptococci deficient in RgfC expression exhibit increased virulence, deletion of rgfC in group B streptococci strains lacking a functional RgfA increased systemic infection. Infection with the rgfC mutant increases induction of proinflammatory signaling pathways in vivo. 19 phosphopeptides corresponding to 12 proteins are differentially phosphorylated at aspartate, cysteine, serine, threonine, or tyrosine residues in the rgfC mutant. This includes aspartate phosphorylation of a tyrosine kinase, CpsD, and a transcriptional regulator. Over 200 genes show altered expression compared to the isogenic wild-type strain and included transcriptional regulators, transporters, and genes previously associated with group B streptococci pathogenesis. In the absence of RgfA, nonspecific RgfC signaling affects the expression of virulence factors and GBS pathogenesis. Sialic acid levels are higher in the DELTArgfCAd mutant than in wild-type A909, correlated with an increase in gene expression of the capsular polysaccharide operon. Sialylation of the group B streptococci capsular polysaccharide is critical for group B streptococci bloodstream infections and pathogenesis
malfunction
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a group A streptococci strain selectively deficient in CovS phosphatase activity has a distinct transcriptome relative to that of its parental strain. Inactivation of CovS in the serotype M1 background results in a greater decrease in phosphorylated CovR levels and a greater increase in the transcript levels of CovR-repressed genes than does CovS inactivation in a serotype M3 strain
malfunction
Streptococcus pyogenes MGAS2221
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a group A streptococci strain selectively deficient in CovS phosphatase activity has a distinct transcriptome relative to that of its parental strain. Inactivation of CovS in the serotype M1 background results in a greater decrease in phosphorylated CovR levels and a greater increase in the transcript levels of CovR-repressed genes than does CovS inactivation in a serotype M3 strain
malfunction
the isogenic chiS mutant (ChiS-) shows less growth compared to the wild-type strain ChiS+ in the presence of mucin supplemented media. The mutant ChiS- strain also shows highly retarded motility as well as mucin layer penetration in vitro
malfunction
binK mutants exhibit a colonization advantage in a global genetic screen, phenotype, overview. Bacterial biofilm aggregates in the host are larger in strains lacking BinK, whereas overexpression of BinK suppresses biofilm formation and squid colonization
malfunction
disruption of Shk1 results in resistance to phenylpyrrole and dicarboximide fungicides and increases sensitivity to hyperosmotic stress and H2O2-induced oxidative stress. The Shk1 mutant shows a significant reduction in vegetative hyphal growth and is unable to produce sclerotia. The Shk1 mutant shows no change in virulence. All the defects are restored by genetic complementation of the Shk1 deletion mutant with the wild-type Shk1 gene
malfunction
the DELTAkinD mutant (and less significantly the DELTAkinC mutant) has the most defective phenotype, while all other kin kinase mutants are able to respond to the addition of GM by forming robust biofilm
malfunction
DeltaHik34 mutant cells are resistant to heat stress within its first hours, they cannot recover after 24 h long high temperature treatment, while the wild-type cell population is able to recover after 24 h of cultivation at 44°C. The damage caused by high temperature depends on many factors, which differ in these experiments: light intensity, CO2 content, the growth stage, or the growth temperature before heat stress. In DELTAHik34 mutant, the content of all pigments starts to decrease after 6 h of heat stress. Heat stress phenotypes, overview
malfunction
in contrast to the wild-type strain, which forms mature pigmented perithecia, only an insignificant number of small unpigmented mutant fruiting bodies are observed in the dcc-1 deletion mutant, thus deletion of dcc-1 leads to sterility. Supplementation with cAMP does not restore the sexual defects (formation of submerged perithecia) of the DELTAdcc-1 mutant
malfunction
impairment of the AaHSK1 gene does not reduce radial growth of the resulting two null mutants (HD1 and HD2) in the presence of tert-butyl-hydroxyperoxide, H2O2, KCl or NaCl, compared to the wild-type. Expression of a functional copy of the AaHSK1 gene in the HD1 null mutant fully restores the altered phenotypes. Deletion of AaHSK1 affects AaHOG1 phosphorylation. Fungal mutants impaired in AaHSK1, AaHOG1, AaAP1 (encoding a redox-responsive transcription factor) or AaFUS3 (encoding a MAP kinase) are all hypersensitive to 2-chloro-5-hydroxypyridine or 2,3,5-triiodobenzoic acid. Glucose enhances AaHOG1 phosphorylation and nuclear localization in the AaHSK1 deficient background. Genetic disruption of the AaHSK1 gene yields fungal strains that are insensitive to dicarboximide (iprodione and vinclozolin) and phenylpyrrole (fludioxonil) fungicides. Inactivation of the AaHSK1 or AaHOG1 gene does not alter the production of host-selective ACT toxin by Alternaria alternata
malfunction
enzyme FimS from W83 is malfunctional. Complementation analysis with chimeric fimS constructs reveals that W83 FimS has a defective kinase domain due to a truncated conserved G3 box motif that provides an ATP-binding pocket. The introduction of the functional fimS from strain ATCC 33277 restores the production, but not polymerization, of endogenous FimA subunits in W83. But even the fimbria-deficient strain W83 retains the ability to polymerize FimA from strain ATCC 33277, indicating the assembly of mature FimA by a primary structure-dependent mechanism. Strain ATCC 33277 FimS-induced W83 FimA is a mature polypeptide and is localized on the cell surface
malfunction
N-terminal truncations of YycG lose negative regulation of their activity, phenotypes, overview. Truncated YycG constructs fail to co-immunoprecipitate with the regulatory proteins YycH and YycI. Deletion or depletion of later stage cell division proteins does not perturb YycG localization
malfunction
loss of function of AHK5 also confers tolerance to high salinity, suggesting that AHK5 acts to integrate multiple stress responses. The AHK5 mutant is more resistant to salt stress, the insensitivity of the ahk5-1 mutant in response to salinity is caused by loss of AHK5 function
malfunction
the female gametophytic lethal phenotype of cki1-5 (a null mutant) can be partially rescued by IPT8 or ARR1 (a type-B Arabidopsis RR) driven by a CKI1 promoter. A mutant allele, cki1-8, is cki1-8 is a weak mutant allele with residual CKI1 expression, and can be transmitted through female gametophytes with low frequency, viable homozygous cki1-8 mutant plants that grow larger than wild-type plants, show defective megagametogenesis, and rarely set enlarged seeds. The cki1-8 mutation impairs female gametophyte development, phenotype overview. Mutant cki1-8 responds normally to cytokinin, remarkably smaller siliques are formed in cki1-8 plants than in the wild type
malfunction
removal of the HAMP or the PAS domain from Hik33n-SphSc and substitutions of amino acid residues in the PAS domain influence kinase activity, overview. Subdomain-deleted variants of Hik33n-SphSc show reduced activity compared to the unaltered chimera
malfunction
gacS or gacA mutations are epistasic to ladS mutation
malfunction
in the absence of LOVHK the expression of the virB operon is downregulated. LOVHK plays a role in the intracellular survival of Brucella, since deletion of this gene in Brucella abortus shows an attenuated phenotype in cell-culture infection assays. PhyR expression is decreased in the lovhk mutant
malfunction
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N-terminal truncations of YycG lose negative regulation of their activity, phenotypes, overview. Truncated YycG constructs fail to co-immunoprecipitate with the regulatory proteins YycH and YycI. Deletion or depletion of later stage cell division proteins does not perturb YycG localization
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malfunction
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loss of function of AHK5 also confers tolerance to high salinity, suggesting that AHK5 acts to integrate multiple stress responses. The AHK5 mutant is more resistant to salt stress, the insensitivity of the ahk5-1 mutant in response to salinity is caused by loss of AHK5 function
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malfunction
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the female gametophytic lethal phenotype of cki1-5 (a null mutant) can be partially rescued by IPT8 or ARR1 (a type-B Arabidopsis RR) driven by a CKI1 promoter. A mutant allele, cki1-8, is cki1-8 is a weak mutant allele with residual CKI1 expression, and can be transmitted through female gametophytes with low frequency, viable homozygous cki1-8 mutant plants that grow larger than wild-type plants, show defective megagametogenesis, and rarely set enlarged seeds. The cki1-8 mutation impairs female gametophyte development, phenotype overview. Mutant cki1-8 responds normally to cytokinin, remarkably smaller siliques are formed in cki1-8 plants than in the wild type
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malfunction
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ectopic CKI1 expression generates non-propagating seeds with dual fertilized endosperms and no embryos. CKI1 loss-of-function mutants exhibit gametophytic defects resulting in semi-sterility. Cell specification is defective in cki1 mutant embryo sacs. Autonomous endosperms arise from ectopic central cells in the PRC2 fis2 (fertilization independent 2) mutant
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malfunction
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in the absence of LOVHK the expression of the virB operon is downregulated. LOVHK plays a role in the intracellular survival of Brucella, since deletion of this gene in Brucella abortus shows an attenuated phenotype in cell-culture infection assays. PhyR expression is decreased in the lovhk mutant
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malfunction
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enzyme FimS from W83 is malfunctional. Complementation analysis with chimeric fimS constructs reveals that W83 FimS has a defective kinase domain due to a truncated conserved G3 box motif that provides an ATP-binding pocket. The introduction of the functional fimS from strain ATCC 33277 restores the production, but not polymerization, of endogenous FimA subunits in W83. But even the fimbria-deficient strain W83 retains the ability to polymerize FimA from strain ATCC 33277, indicating the assembly of mature FimA by a primary structure-dependent mechanism. Strain ATCC 33277 FimS-induced W83 FimA is a mature polypeptide and is localized on the cell surface
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malfunction
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the isogenic chiS mutant (ChiS-) shows less growth compared to the wild-type strain ChiS+ in the presence of mucin supplemented media. The mutant ChiS- strain also shows highly retarded motility as well as mucin layer penetration in vitro
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malfunction
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binK mutants exhibit a colonization advantage in a global genetic screen, phenotype, overview. Bacterial biofilm aggregates in the host are larger in strains lacking BinK, whereas overexpression of BinK suppresses biofilm formation and squid colonization
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malfunction
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disruption of Shk1 results in resistance to phenylpyrrole and dicarboximide fungicides and increases sensitivity to hyperosmotic stress and H2O2-induced oxidative stress. The Shk1 mutant shows a significant reduction in vegetative hyphal growth and is unable to produce sclerotia. The Shk1 mutant shows no change in virulence. All the defects are restored by genetic complementation of the Shk1 deletion mutant with the wild-type Shk1 gene
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malfunction
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in contrast to the wild-type strain, which forms mature pigmented perithecia, only an insignificant number of small unpigmented mutant fruiting bodies are observed in the dcc-1 deletion mutant, thus deletion of dcc-1 leads to sterility. Supplementation with cAMP does not restore the sexual defects (formation of submerged perithecia) of the DELTAdcc-1 mutant
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malfunction
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impairment of the AaHSK1 gene does not reduce radial growth of the resulting two null mutants (HD1 and HD2) in the presence of tert-butyl-hydroxyperoxide, H2O2, KCl or NaCl, compared to the wild-type. Expression of a functional copy of the AaHSK1 gene in the HD1 null mutant fully restores the altered phenotypes. Deletion of AaHSK1 affects AaHOG1 phosphorylation. Fungal mutants impaired in AaHSK1, AaHOG1, AaAP1 (encoding a redox-responsive transcription factor) or AaFUS3 (encoding a MAP kinase) are all hypersensitive to 2-chloro-5-hydroxypyridine or 2,3,5-triiodobenzoic acid. Glucose enhances AaHOG1 phosphorylation and nuclear localization in the AaHSK1 deficient background. Genetic disruption of the AaHSK1 gene yields fungal strains that are insensitive to dicarboximide (iprodione and vinclozolin) and phenylpyrrole (fludioxonil) fungicides. Inactivation of the AaHSK1 or AaHOG1 gene does not alter the production of host-selective ACT toxin by Alternaria alternata
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malfunction
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residue 293 plays a central role in the altered structural specificity of the DELTA280-293 truncation, activation of VirA by phenols increases in the absence of enzyme aas 285-293. Mutations in the L domain can rescue null mutants in the R domain. Y293F substitution switches VirA from requiring two separate inputs to an OR gate, responding to both signals separately
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metabolism
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DcuS and CitA are involved in the regulation of carboxylate metabolism
metabolism
proposed signal transduction pathway for the Hik2-based two-component system in cyanobacteria, overview
metabolism
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compared to a serotype M3 strain, serotype M1 GAS strains have high levels of phosphorylated CovR, low transcript levels of CovR-repressed genes, and strikingly different responses to environmental cues. Genetic inactivation of covS decreases but does not eliminate CovR phosphorylation
metabolism
Streptococcus pyogenes MGAS2221
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compared to a serotype M3 strain, serotype M1 GAS strains have high levels of phosphorylated CovR, low transcript levels of CovR-repressed genes, and strikingly different responses to environmental cues
metabolism
five distinct sensor kinases (KinA, KinB, KinC, KinD, and KinE) have the capability of transferring a phosphoryl group into the phosphorelay to control the level of phosphorylated transcriptional regulator Spo0A present at any moment in the cell
metabolism
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in response to starvation, Bacillus subtilis cells differentiate into different subsets, undergoing cannibalism, biofilm formation or sporulation. These processes require a multiple component phosphorelay, wherein the master regulator Spo0A is activated upon phosphorylation by one or a combination of five histidine kinases (KinA-KinE) via two intermediate phosphotransferases, Spo0F and Spo0B. KinC controls the expression of cannibalism genes in a manner independent of surfactin andthe bacterial flotillin-like proteins FloT and FloA
metabolism
biofilm formation depends on the synthesis of an extracellular matrix, which is indirectly regulated by the transcriptional regulator Spo0A. The activity of Spo0A depends on its phosphorylation state. Low and intermediate levels of phosphorylated Spo0A lead to induction of the epsA-O and tapA operons, which results in production of the extracellular matrix and thus biofilm formation, while at high levels, the matrix genes are repressed. The level of phosphorylated Spo0A is controlled by a network of kinases and phosphatases, which respond to environmental and physiological signals. Biofilm formation of Bacillus subtilis in LB medium is triggered by a combination of glycerol and manganese via KinD sensoring. The kinase KinD contains an extracellular domain, so called CACHE domain, for sensing small chemical molecules released from plant host during colonization. The glpK-encoded glycerol kinase and glpF encoded glycerol transport facilitator are critical in utilization of glycerol as a carbon source
metabolism
the AaHOG1-mediated pathway confers cellular resistance to salts and oxidative stress and bypasses AaHSK1. Accumulation of the AaHSK1 gene transcript is negatively regulated by AaHOG1, AaAP1 or AaFUS3. AaHOG1 is necessary for fungal pathogenicity, yet AaHSK1 is completely dispensable for pathogenicity. AaHSK1 functions in osmotic tolerance without involving AaHOG1. Relationships between the HOG1 MAP kinase and the histidine kinase in Alternaria alternata, overview
metabolism
gene CKI1 is part of the genetic pathway consisting of CKI1, AHPs, and type-B ARRs in the regulation of female gametophyte development and vegetative growth
metabolism
the functional form of Hik2 is a higher-order oligomer such as a hexamer or octamer. The monomer, tetramer and hexamer forms of Hik2 are autokinase-active. Increased NaCl concentrations convert the active hexamer into an inactive tetramer. The action of NaCl appears to be confined to the Hik2 kinase domain
metabolism
the expression level of ohkAsp exerts different effects on the transcriptional level of genes responsible for regulation of doxorubicin/daunorubicin production, efflux system, cofactor supply and developmental genes
metabolism
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five distinct sensor kinases (KinA, KinB, KinC, KinD, and KinE) have the capability of transferring a phosphoryl group into the phosphorelay to control the level of phosphorylated transcriptional regulator Spo0A present at any moment in the cell
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metabolism
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in response to starvation, Bacillus subtilis cells differentiate into different subsets, undergoing cannibalism, biofilm formation or sporulation. These processes require a multiple component phosphorelay, wherein the master regulator Spo0A is activated upon phosphorylation by one or a combination of five histidine kinases (KinA-KinE) via two intermediate phosphotransferases, Spo0F and Spo0B. KinC controls the expression of cannibalism genes in a manner independent of surfactin andthe bacterial flotillin-like proteins FloT and FloA
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metabolism
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gene CKI1 is part of the genetic pathway consisting of CKI1, AHPs, and type-B ARRs in the regulation of female gametophyte development and vegetative growth
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metabolism
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the expression level of ohkAsp exerts different effects on the transcriptional level of genes responsible for regulation of doxorubicin/daunorubicin production, efflux system, cofactor supply and developmental genes
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metabolism
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the AaHOG1-mediated pathway confers cellular resistance to salts and oxidative stress and bypasses AaHSK1. Accumulation of the AaHSK1 gene transcript is negatively regulated by AaHOG1, AaAP1 or AaFUS3. AaHOG1 is necessary for fungal pathogenicity, yet AaHSK1 is completely dispensable for pathogenicity. AaHSK1 functions in osmotic tolerance without involving AaHOG1. Relationships between the HOG1 MAP kinase and the histidine kinase in Alternaria alternata, overview
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physiological function
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histidine kinase KinA promotes the initiation of sporulation when nutrients are limiting
physiological function
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the AgrC receptor histidine kinase detects its autoinducing peptide ligand and generates an intracellular signal resulting in secretion of virulence factors
physiological function
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NikA is responsible for the responses to fungicides such as iprodione and fludioxonil, NikA functions as sensor upstream of the response regulators SskA and SrrA in response to fungicides
physiological function
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histidine kinase Chk1p HK is part of a functionally similar but parallel pathway to the Sho1p-Cek1p pathway that confers resistance to the cell wall inhibitors Congo red and calcofluor white
physiological function
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CckA has a central role in establishing the cell cycle periodicity of CtrA activity by controlling both its phosphorylation and stability
physiological function
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HP0244 is required for inner membrane assembly of UreA, UreB, and UreE and for urease activity
physiological function
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the VirA receiver domain is required for efficient vir gene expression, including the transcriptional induction of virG, VirA's receiver domain acts as a recruitment and/or alignment factor that increases the availability of VirG for phosphate transfer from VirA's kinase region to the VirG receiver domain
physiological function
the NIK1 gene is involved in ambruticin susceptibility
physiological function
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the histidine kinase SphS is involved in transcriptional activation of the phosphate (Pi)-acquisition system
physiological function
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FixL utilizes a heme bound to an N-terminal PAS domain to detect the amount of oxygen present in the cytoplasm through direct binding
physiological function
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KdpD regulates the expression of potassium transporters in response to osmolarity
physiological function
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HHK1 regulates polar growth, sporulation, and cell wall composition
physiological function
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cytokinin-independent1 and Arabidopsis histidine kinase2 and 3 regulate vascular tissue development in Arabidopsis shoots, the cytokinin-independent activity of CKI1 and cytokinin-induced histidine kinase2 and histidine kinase3 are important for vascular bundle formation in Arabidopsis
physiological function
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the histidine kinase-related domain of phytochrome A controls the spectral sensitivity and the subcellular distribution of the photoreceptor
physiological function
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functional HK5 histidine kinase is required for H2O2 responses in stomatal guard cells
physiological function
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the TorS histidine kinase activates the trimethylamine-N-oxide reductase pathway when sensing trimethylamine-N-oxide in the environment
physiological function
the TorS histidine kinase activates the trimethylamine-N-oxide reductase pathway when sensing trimethylamine-N-oxide in the environment
physiological function
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histidine kinase Ppr functions as a UV-red light sensor
physiological function
Hik2 is the cytoplasmic homologue of chloroplast sensor kinase (CSK), a protein involved in redox regulation of chloroplast gene expression during changes in light quality in plants and algae. Hik2 is the sensor that acts on Rre1 and RppA transcription factors to regulate photosynthesis genes as part of the mechanism of photosystem stoichiometry adjustment in cyanobacteria. Signaling mechanism of Hik2 and its phosphotransferase activity, overview. Hik2-based signaling pathway integrates acclimatory responses to light and salt stresses in cyanobacteria
physiological function
DraK is a sensory histidine kinase involved in the differential regulation of antibiotics in Streptomyces coelicolor through the DraR/DraK two-component system
physiological function
in bacteria, two-component systems act as signaling systems to respond to environmental stimuli. Two-component systems generally consist of a sensor histidine kinase and a response regulator, which work together through histidyl-aspartyl phospho-relay to result in gene regulation. One of the two-component systems in Escherichia coli, CusS-CusR, is known to induce expression of cusCFBA genes under increased periplasmic Cu(I) and Ag(I) concentrations to help maintain metal ion homeostasis. CusS senses increasing metal ion concentrations and activates CusR. ATP-dependent auto-phosphorylation occurs at a conserved His residue in the kinase core. The phosphoryl group is then transferred from the histidine kinase to a conserved Asp residue on the N-terminal receiver domain of the response regulator, which in turn activates the C-terminal effector domain to mediate an adaptive response. The phosphorylated response regulator activates transcription of genes that respond to the environmental stimulus. Analysis of the molecular role of CusS in Cu(I)/Ag(I) resistance and the mechanism of CusS signal transduction in Escherichia coli, overview. In response to periplasmic Ag(I) and Cu(I), CusS upregulates the genes to express the CusCBA Cu(I)/Ag(I) efflux pump to remove excess metal ions from the cell
physiological function
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the globin-coupled histidine kinase, AfGcHK, is a part of the two-component signal transduction system. Activation of its sensor domain significantly increases its autophosphorylation activity, which targets the His183 residue of its functional domain. The phosphate group of phosphorylated AfGcHK is then transferred to the cognate response regulator
physiological function
CusS is a prototypical periplasmic sensing histidine kinase, the histidine kinase CusS of the CusRS two-component system functions as a Ag(I)/Cu(I)-responsive sensor kinase and is essential for induction of the genes encoding the CusCFBA efflux pump. CusS has an important role in silver resistance and regulation of copper homeostasis
physiological function
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Ti plasmid-encoded two-component signaling system, designated VirA and VirG, where VirA serves as the histidine autokinase antenna that phosphorylates VirG as the active transcriptional regulator. Histidine kinase VirA processes multiple small molecule host signals (phenol and sugar) and is essential for pathogenesis of Rhizobium radiobacter. A single residue can switch enzyme VirA from a functional AND logic gate to an OR gate where each of two signals activate independently. Host range preferences among natural strains of Rhizobium radiobacter correlate with these gate logic strategies. VirA, which exists in the inner membrane as a homodimer, is composed of multiple domains assigned as periplasmic (P), linker (L), kinase (K), and receiver (R). Sugar perception requires the P domain, whereas phenols require the L domain, localizing detection of these small molecules to opposite sides of the inner membrane. Importance of the integration node, specifically residue 293, as critical for signaling. In most natural isolates, including the frequently used A6 and C58 strains, the wild-type residue for 293 is tyrosine, but in strains Ag162, AB2/73, and KU12, the residue at 293 is phenylalanine. Strains A6, C58, and KU12 are wide-host-range pathogens, whereas strains Ag162 and AB2/73 show limited host ranges
physiological function
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Arabidopsis thaliana endosperm formation requires the cytokinin independent 1 (CKI1) histidine kinase, an activator of the cytokinin signaling pathway, which specifies central cells and restricts egg cell fate. Seeds of flowering plants contain embryos and nutritive endosperm arising from double fertilization of two dimorphic female gametes. The key to specification of only one female gamete for endosperm formation is the regulated localization of the CKI1 histidine kinase by expression control and protein translocation. Dimorphism of the two adjacent gametes is mechanistically established in the syncytial embryo sac by spatially restricted CKI1 expression, followed by translocation of endoplasmic reticulum-localized CKI1 protein via nuclear migration. CKI1-directed specification of the endosperm precursor central cell results in seeds containing an embryo and an endosperm, mechanism, overview
physiological function
Hik2 is one of three essential histidine kinases in the cyanobacterium Synechocystis sp. PCC 6803. The signal input domain of Hik2 responds to environmental Cl- concentration
physiological function
A0A8G2N576
the two-component system comprising the sensor histidine kinase RgfC and the response regulator RgfA mediate GBS binding to extracellular matrix components, such as fibrinogen. The sensor histidine kinase RgfC is involved in gene regulation in group B streptococci and affects group B streptococcal virulence factor expression independent of its response regulator RgfA. Enzyme RgfC regulates expression of capsular polysaccharide and serine protease genes in GBS A909. RgfC functions as a nonspecific or orphan kinase in group B streptococci strains
physiological function
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two-component gene regulatory systems (TCSs) are a major mechanism by which bacteria respond to environmental stimuli and are critical to infectivity. The control of virulence regulator/sensor kinase (CovRS) TCS is central to the virulence of the major human pathogen group A Streptococcus (GAS). In the system, the histidine kinase CovS primarily serves to phosphorylate CovR, thereby resulting in the repression of virulence factor-encoding genes. Both CovS kinase and phosphatase activities influence the CovR phosphorylation status. Serotype M1 GAS strains have high rates of spontaneous mutations in covS during invasive GAS infection, thus providing a link between TCS molecular function and the epidemiology of deadly bacterial infections
physiological function
Streptococcus pyogenes MGAS2221
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two-component gene regulatory systems (TCSs) are a major mechanism by which bacteria respond to environmental stimuli and are critical to infectivity. The control of virulence regulator/sensor kinase (CovRS) TCS is central to the virulence of the major human pathogen group A Streptococcus (GAS). In the system, the histidine kinase CovS primarily serves to phosphorylate CovR, thereby resulting in the repression of virulence factor-encoding genes. Both CovS kinase and phosphatase activities influence the CovR phosphorylation status. Serotype M1 GAS strains have high rates of spontaneous mutations in covS during invasive GAS infection, thus providing a link between TCS molecular function and the epidemiology of deadly bacterial infections
physiological function
role of a sensor histidine kinase ChiS as an regulator in pathogenesis. The enzyme regulates the chitin utilization pathway and the associated two required factors, chitin binding protein and chitinases, like ChiA2. Enzyme ChiS is important for adherence and survival in HT-29 cells. ChiS is an important factor for utilizing mucin as a sole nutrient source. Cell adhesion, motility, and mucin penetration depends on ChiS. ChiS affects suckling mice colonization in mice and contributes in fluid accumulation as well as colonization in rabbit intestine
physiological function
the activity of transcriptional regulator Spo0A depends on its phosphorylation state. The level of phosphorylated Spo0A is controlled by a network of kinases and phosphatases, which respond to environmental and physiological signals. KinD is a principal histidine kinase responsible for sensing the presence of glycerol and manganese, which trigger biofilm formation of Bacillus subtilis in LB medium, exclusively by its extracellular CACHE sensor domain. The biofilm-promoting effect of glycerol and manganese is mediated mainly by the histidine kinase KinD
physiological function
two-component signal transduction systems (TCSs) in bacteria perceive environmental stress and transmit the information via phosphorelay to adjust multiple cellular functions for adaptation. The EvgS/EvgA system is a TCS that confers acid resistance to Escherichia coli cells. Activation of the EvgS sensor initiates a cascade of transcription factors, EvgA, YdeO, and GadE, which induce the expression of a large group of acid resistance genes
physiological function
gene VF_A0360 encodes the biofilm inhibitor kinase binK, an orphan hybrid histidine kinase that negatively regulates the Vibrio fischeri symbiotic biofilm (Syp) in vivo and in vitro. Colonization of Euprymna scolopes bobtail squid by Vibrio fischeri bacteria requires bacterial aggregation in host mucus as the symbiont transitions from a planktonic lifestyle in seawater to a biofilm-associated state in the host. Enzyme BinK acts upstream of SypG, the sigma54-dependent transcriptional regulator of the syp biofilm locus. The BinK effects are dependent on intact signaling in the RscS-Syp biofilm pathway. Enzyme BinK antagonizes the signal from RscS and serves as an integral component in Vibrio fischeri biofilm regulation. The hybrid histidine kinase BinK is a negative regulator of in vivo aggregation and squid colonization and of Syp biofilm phenotypes in culture. BinK is acting through SypG and not SypE
physiological function
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CheA differs from sensor histidine kinases in several ways: CheA does not contain a transmembrane domain, relying instead on P5 and CheW for interaction with transmembrane components. It has the phosphorylatable His residue on a separate domain (P1) instead of the dimerization domain (P3), and it utilizes a separate docking domain (P2) for CheY. P2 is not necessary for phosphotransfer to the response regulator CheY per se but variants lacking the P2 domain (DELTAP2) exhibit a reduced phosphotransfer rate relative to full-length CheA (CheAFL) and support a lower extent of chemotaxis. The linkers between the CheA domains play important roles in CheA activity
physiological function
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in response to light, as part of a two-component system, the Brucella blue light-activated histidine kinase (LOV-HK) increases its autophosphorylation, modulating the virulence of this microorganism
physiological function
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enzyme KinC regulates cannibalism and biofilm formation, and activates the expression of cannibalism genes in response to starvation in a manner dependent on phosphorelay. KinC activity and the membrane localization are independent of both the lipid raft marker proteins FloTA and cytoplasmic potassium concentration. KinC becomes active by forming a homotetramer via the N-terminal PAS domain
physiological function
two-component histidine kinases (HKs) regulate responses to environmental stimuli in bacteria and eukaryotes, including yeasts, plants, slime moulds and filamentous fungi. Fungal histidine kinases are involved in osmotic and oxidative stress responses, hyphal development, fungicide sensitivity and virulence. The two-component histidine kinase Shk1 controls stress response, sclerotial formation and fungicide resistance in Sclerotinia sclerotiorum. The expression of SsHOG1 (the last kinase of the Hog pathway) and glycerol accumulation are regulated by the Shk1 gene, but PAK (p21-activated kinase) is not
physiological function
KinD is a principal histidine kinase for sensing the presence of GM, exclusively by its extracellular CACHE domain. A combination of glycerol and manganese promotes multicellular development by Bacillus subtilis. The strong biofilm-stimulating activity in response to the addition of a combination of glycerol and manganese is indeed due to upregulation of the matrix genes mediated mainly by the histidine kinase KinD
physiological function
the enzyme Hik34 plays an important role in changes in transcriptome, proteome, lipidome, and photosynthesis in response to short term heat stress. Hik34 affects the expression of sets of genes under salt and osmotic stress, under normal conditions and heat stress and under oxidative stress
physiological function
one of the main components of two-component systems, TCSs, is a sensor histidine kinase, which relays extracellular signals to intracellular pathways. VicK is an important sensor histidine kinase in the tooth decay pathogen Streptomyces mutans
physiological function
the DraR/DraK two-component system (TCS) of Streptomyces coelicolor is involved in the differential regulation of antibiotic biosynthesis. The extracellular sensory domain of histidine kinase DraK shows a pH-dependent conformational change involved in signal transduction process of DraR/DraK TCS. At low pH, the extracellular sensory domain is more structured than that at high pH. In particular, the glutamate at position 83 is an important residue for the pH-dependent conformational change
physiological function
two-component signaling pathways are based on phosphoryl group transfer between histidine kinase and response regulator proteins and regulate environmental responses. The DCC-1 protein in Neurospora crasse protein participates in the regulation of processes such as conidiation, perithecial development, and, to a certain degree, carotenogenesis. DCC-1 exerts its effect by promoting cyclic AMP production, including GNA-3 and CR-1, thereby placing this protein within the context of a signaling pathway that operates during conidiation and sexual development. The DCC-1 histidine kinase is required for proper perithecial development, it has a significant role as a negative regulator of sporulation during vegetative growth
physiological function
AaHSK1 is a primary regulator for cellular resistance to sugar osmotic stress and for sensitivity to dicarboximide or phenylpyrrole fungicides. Important role of AaHSK1 in osmotic adaption, specifically to sugar osmoticants. AaHSK1 does not play an essential role in fungal pathogenicity
physiological function
the FimA-related gene cluster (the fim gene cluster) is positively regulated by the FimS-FimR two-component system. The assembly of mature FimA by a primary structure-dependent mechanism. FimSR is the unique and universal regulatory system that activates the fim gene cluster in a fimA genotype-independent manner
physiological function
DesK is a sensor histidine kinase that allows Bacillus subtilis to respond to cold shock, triggering the adaptation of membrane fluidity via transcriptional control of a fatty acid desaturase. The transmembrane region can sense temperature-modulated fluidity changes of lipid bilayers, transmitting the signal toward the C-terminal cytoplasmic catalytic core of about 220 residues. The cold thermal stimulus is detected by DesK, which then interacts with its cognate response regulator, DesR, constituting a canonical two-component system, TCS
physiological function
The enzyme YycG is part of the two-component signal transduction system YycFG or WalRK. The YycG (WalK) sensor histidine kinase coordinates cell wall remodeling with cell division in Gram-positive bacteria by controlling the transcription of genes for autolysins and their inhibitors. The essential enzyme YycG senses cell division and is enzymatically activated by associating with the divisome at the division septum. The cytoplasmic PAS domain of this multidomain trans-membrane kinase is a determining factor translocating the kinase to the division septum. YycG activity in non-dividing cells is suppressed by its interaction with YycH and YycI and its activation is coordinated to cell division in dividing cells by specific interactions that occur within the divisome. This regulation is accomplished through its transmembrane and extra-membrane domains interacting with the membrane associated YycH and YycI proteins that do not localize to the divisome. Signaling by YycG involves later stage cell division proteins, overview
physiological function
the hybrid histidine kinase Arabidopsis histidine kinase 5 (AHK5) mediates stomatal responses to exogenous and endogenous signals in Arabidopsis thaliana, AHK5 integrates abiotic and biotic stimuli in stomatal guard cells through regulation of H2O2 homeostasis. Role for AHK5 in the regulation of survival following challenge by a hemi-biotrophic bacterium and a necrotrophic fungus, as well as in the growth response to salt stress. AHK5 positively regulates salt sensitivity and contributes to resistance to the bacterium Pseudomonas syringae pv. tomato DC3000 and the fungal pathogen Botrytis cinerea, detailed overview. Function of AHK5 in regulating the production of hormones and redox homeostasis. Enzyme AHK5 functions as a negative regulator of root growth inhibition mediated by abscisic acid/ethylene. AHK5 positively regulates salt-induced root growth inhibition
physiological function
cytokinin signaling is mediated by a multiple-step phosphorelay. Key components of the phosphorelay consist of the histidine kinase (HK)-type receptors, histidine phosphotransfer proteins (HP), and response regulators (RRs). Histidine kinase CKI1 acts upstream of histidine phosphotransfer proteins to regulate female gametophyte development and vegetative growth, role of AHP proteins in female gametophyte development, overview
physiological function
histidine kinase Hik33 is one of the key regulators helping Synechocystis acclimate to multiple stress conditions, Hik33 may play important roles in allowing cells to acclimate to changing environmental conditions
physiological function
histidine kinase SphS senses phosphate-deficient conditions. SphS phosphorylates its cognate response regulator, SphR, under phosphate-deficient conditions and regulates the expression of the so-called pho regulon, which includes genes for acclimation to phosphate-deficient conditions, namely genes for a periplasmic alkaline phosphatase PhoA and phosphate transporters
physiological function
in response to environmental changes, Pseudomonas aeruginosa is able to switch from a planktonic (free swimming) to a sessile (biofilm) lifestyle. The two-component system GacS/GacA activates the production of two small non-coding RNAs, RsmY and RsmZ, but four histidine kinases, RetS, GacS, LadS and PA1611, are instrumental in this process. RetS hybrid histidine kinase blocks GacS unorthodox histidine kinase autophosphorylation through the formation of a heterodimer. PA1611 hybrid histidine kinase, which is structurally related to GacS, interacts with RetS in Pseudomonas aeruginosa in a very similar manner to GacS. LadS hybrid histidine kinase phenotypically antagonizes the function of RetS by a mechanism that has never been investigated. The four sensors are found in most Pseudomonas species but their characteristics and mode of signaling may differ from one species to another. In Pseudomonas aeruginosa, LadS controls both rsmY and rsmZ gene expression and this regulation occurs through the GacS/GacA two-component system. In contrast to RetS, LadS signals through GacS/GacA without forming heterodimers, either with GacS or with RetS. Enzyme LadS is involved in a genuine phospho relay, which requires both transmitter and receiver LadS domains. LadS signaling ultimately requires the alternative histidine-phosphotransfer domain of GacS. LadS histidine kinase forms, with the GacS/GacA two-component system, a multicomponent signal transduction system with an original phosphorelay cascade, i.e. H1LadS -> D1LadS -> H2GacS -> D2GacA. This highlights an original strategy in which a unique output, i.e. the modulation of sRNA levels, is controlled by a complex multi-sensing network to fine-tune an adapted biofilm and virulence response. H1 and D1 domain involvement of the LadS hybrid histidine kinase in the LadS signaling pathway, and involvement of the H2 domain of the GacS unorthodox histidine kinase in the LadS signaling pathway, overview
physiological function
in response to environmental changes, Pseudomonas aeruginosa is able to switch from a planktonic (free swimming) to a sessile (biofilm) lifestyle. The two-component system GacS/GacA activates the production of two small non-coding RNAs, RsmY and RsmZ, but four histidine kinases, RetS, GacS, LadS and PA1611, are instrumental in this process. RetS hybrid histidine kinase blocks GacS unorthodox histidine kinase autophosphorylation through the formation of a heterodimer. PA1611 hybrid histidine kinase, which is structurally related to GacS, interacts with RetS in Pseudomonas aeruginosa in a very similar manner to GacS. LadS hybrid histidine kinase phenotypically antagonizes the function of RetS. The four sensors are found in most Pseudomonas species but their characteristics and mode of signaling may differ from one species to another. In Pseudomonas aeruginosa, LadS controls both rsmY and rsmZ gene expression and this regulation occurs through the GacS/GacA two-component system. In contrast to RetS, LadS signals through GacS/GacA without forming heterodimers, either with GacS or with RetS. Enzyme LadS is involved in a genuine phospho relay, which requires both transmitter and receiver LadS domains. LadS signaling ultimately requires the alternative histidine-phosphotransfer domain of GacS. LadS histidine kinase forms, with the GacS/GacA two-component system, a multicomponent signal transduction system with an original phosphorelay cascade, i.e. H1LadS -> D1LadS -> H2GacS -> D2GacA. This highlights an original strategy in which a unique output, i.e. the modulation of sRNA levels, is controlled by a complex multi-sensing network to fine-tune an adapted biofilm and virulence response. In vitro transphosphorylation of GacS H2 domain by LadS histidine kinase, involvement of the H2 domain of the GacS unorthodox histidine kinase in the LadS signaling pathway
physiological function
the DraR/DraK two-component system is involved in the differential regulation of antibiotic biosynthesis in a medium-dependent manner, the DraR/DraK two-component system plays an important role in the pH regulation of Streptomyces coelicolor growth medium. The enzyme and the DraR/DraK two-component system are essential for the recovery of the pH of Streptomyces coelicolor growth medium after acid shock, overview
physiological function
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the integral membrane protein AgrC is a histidine kinase whose sensor domains interact with an autoinducing peptide, resulting in a series of downstream responses
physiological function
LOV histidine kinase positively regulates the general stress response system and affects the virB operon expression in Brucella abortus. The Brucella genome encodes a sensor histidine kinase containing a LOV domain upstream from the kinase, LOVHK, which plays an important role in light-regulated Brucella virulence. The intracellular signaling pathway is initiated by the light sensor LOVHK, which functionally interacts with two response regulators: PhyR and LovR, constituting a functional two-component signal-transduction system. LOVHK contributes to the activation of the general stress response (GSR) system in Brucella via PhyR, the main regulator of the general stress response system, while LovR is proposed to be a phosphate-sink for LOVHK, decreasing its phosphorylation state. LOVHK plays a role in the intracellular survival of Brucella and in defense of stress induced by starvation. LOVHK signaling cascade, overview
physiological function
CheA is a central component of the chemotaxis signal transduction pathway that allows prokaryotic cells to control their movements in response to environmental cues
physiological function
a CPR0195 null mutant makes 1000fold fewer spores than its wild-type parent and produces no detectable enterotoxin. CPR0195 functions early during sporulation, i.e., prior to production of sporulation-associated sigma factors. The CPR0195 kinase domain can autophosphorylate and phosphorylate Spo0A
physiological function
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TcsC is required for wild-type-like growth on Czapek-Dox medium and a normal resistance to certain oxidative stressors. An increased resistance to the cell wall disturbing agents Congo red and Calcofluor white is found for the TcsC mutant
physiological function
Q5B4Q1
isoform NikA is required for wild-type-like growth on Czapek-Dox medium and a normal resistance to certain oxidative stressors. A NikA mutant grows well in the presence of 1 microg/ml fludioxonil, whereas the wild-type strain is severely impaired in growth. In the presence of fludioxonil, the NikA mutant forms fluffy and often white colonies. Resting conidia of the NikA mutant retain their viability during storage at 4°C
physiological function
MHZ1 is autophosphorylated at a conserved histidine residue and can transfer the phosphoryl signal to the response regulator RR21 via the phosphotransfer proteins AHP1/2. This phosphorelay pathway is required for root ethylene responses. Ethylene receptor ERS2, via its GAF domain, physically interacts with MHZ1 and inhibits its kinase activity. MHZ1 acts at the level of ethylene perception and works together with the EIN2-mediated pathway to regulate root growth. MHZ1 overexpression enhances ethylene response in roots
physiological function
free-standing PilZ protein PA2799 interacts directly with the histidine kinase SagS. PA2799 binds directly to the phosphoreceiver domain of SagS, and the SagS-HapZ interaction is further enhanced at elevated c-di-GMP concentration. Binding of HapZ to SagS inhibits the phosphotransfer between SagS and the downstream protein HptB in a c-di-GMP-dependent manner. HapZ impacts surface attachment and biofilm formation most likely by regulating the expression of a large number of genes
physiological function
NME1 depletion impacts migration and differentiation but not proliferation in neuroblastoma cells. Candidate targets of NME1 histidine kinase activity include ENO1, GAPDH, and PKM
physiological function
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repression of HK1 impairs cell specification in the central endosperm transfer cell region and the development of transfer cell morphology, and consecutively defects differentiation of adjacent endosperm tissues. Concomittantly, disturbed cell plate formation and fusion are observed at the initiation of endosperm cellularization, loss of transfer cell identity, compromised cell wall biogenesis and reduced transport capacities in aberrant cells and elucidated two-component signaling and hormone pathways that are mediated by HK1. Non-canonical auxin signaling elements are predicted as direct targets of HvHK1 as the main regulatory links governing cellularization of endosperm transfer cells
physiological function
a helix linking the transmembrane region with the cytoplasmic catalytic domain is involved in DesK pH sensing. This helix contains several glutamate, lysine, and arginine residues At neutral pH, the linker forms an alpha helix that is stabilized by hydrogen bonds in the i, i + 4 register and favors the kinase state. At low pH, protonation of glutamate residues breaks salt bridges, which results in helix destabilization and interruption of signaling. This mechanism inhibits unsaturated fatty acid synthesis and rigidifies the membrane when Bacillus subtilis grows in acidic conditions
physiological function
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sporangia of an HhkA deletion mutant contain many distorted or ectopically germinated spores and scarcely open to release the spores under sporangium dehiscence-inducing conditions. HhkA regulates a signal transduction pathway involved in sporangium formation, spore dormancy, and sporangium dehiscence. Genes regulated by HhkA overlap mostly with global transcriptional activator TcrA-regulated genes. The interaction between HhkA and TcrA is very weak and probably transient
physiological function
an allosteric switching mechanism may involve two autophosphorylation and two phosphotransfer reactions. The CpxR-mediated allosteric control of the autophosphorylation reaction ensures that the large-scale domain movements proceed in a coordinated way along the cycle, thus optimizing the overall catalytic efficiency
physiological function
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outer-membrane lipoprotein RcsF interacts with the periplasmic domain of the innermembrane-localized histidine kinase RcsC (RcsCperi). RcsCperi, when secreted to the periplasm by fusion to maltose-binding protein, titrates RcsF's activating effect. Deletions in the periplasmic domain of RcsC abolish the activation effect of RcsF
physiological function
a GacS mutant devoid of the periplasmic detector domain is severely defective in biofilm formation accompanied by concomitant changes in the expression of small RNAs RsmY/Z that control activation of GacA-regulated genes. Point mutations in a putative ligand binding pocket lined by positively-charged residues originating primarily from the major loop impair biofilm formation
physiological function
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the activity of transcriptional regulator Spo0A depends on its phosphorylation state. The level of phosphorylated Spo0A is controlled by a network of kinases and phosphatases, which respond to environmental and physiological signals. KinD is a principal histidine kinase responsible for sensing the presence of glycerol and manganese, which trigger biofilm formation of Bacillus subtilis in LB medium, exclusively by its extracellular CACHE sensor domain. The biofilm-promoting effect of glycerol and manganese is mediated mainly by the histidine kinase KinD
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physiological function
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KinD is a principal histidine kinase for sensing the presence of GM, exclusively by its extracellular CACHE domain. A combination of glycerol and manganese promotes multicellular development by Bacillus subtilis. The strong biofilm-stimulating activity in response to the addition of a combination of glycerol and manganese is indeed due to upregulation of the matrix genes mediated mainly by the histidine kinase KinD
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physiological function
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DesK is a sensor histidine kinase that allows Bacillus subtilis to respond to cold shock, triggering the adaptation of membrane fluidity via transcriptional control of a fatty acid desaturase. The transmembrane region can sense temperature-modulated fluidity changes of lipid bilayers, transmitting the signal toward the C-terminal cytoplasmic catalytic core of about 220 residues. The cold thermal stimulus is detected by DesK, which then interacts with its cognate response regulator, DesR, constituting a canonical two-component system, TCS
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physiological function
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The enzyme YycG is part of the two-component signal transduction system YycFG or WalRK. The YycG (WalK) sensor histidine kinase coordinates cell wall remodeling with cell division in Gram-positive bacteria by controlling the transcription of genes for autolysins and their inhibitors. The essential enzyme YycG senses cell division and is enzymatically activated by associating with the divisome at the division septum. The cytoplasmic PAS domain of this multidomain trans-membrane kinase is a determining factor translocating the kinase to the division septum. YycG activity in non-dividing cells is suppressed by its interaction with YycH and YycI and its activation is coordinated to cell division in dividing cells by specific interactions that occur within the divisome. This regulation is accomplished through its transmembrane and extra-membrane domains interacting with the membrane associated YycH and YycI proteins that do not localize to the divisome. Signaling by YycG involves later stage cell division proteins, overview
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physiological function
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enzyme KinC regulates cannibalism and biofilm formation, and activates the expression of cannibalism genes in response to starvation in a manner dependent on phosphorelay. KinC activity and the membrane localization are independent of both the lipid raft marker proteins FloTA and cytoplasmic potassium concentration. KinC becomes active by forming a homotetramer via the N-terminal PAS domain
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physiological function
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a helix linking the transmembrane region with the cytoplasmic catalytic domain is involved in DesK pH sensing. This helix contains several glutamate, lysine, and arginine residues At neutral pH, the linker forms an alpha helix that is stabilized by hydrogen bonds in the i, i + 4 register and favors the kinase state. At low pH, protonation of glutamate residues breaks salt bridges, which results in helix destabilization and interruption of signaling. This mechanism inhibits unsaturated fatty acid synthesis and rigidifies the membrane when Bacillus subtilis grows in acidic conditions
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physiological function
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the hybrid histidine kinase Arabidopsis histidine kinase 5 (AHK5) mediates stomatal responses to exogenous and endogenous signals in Arabidopsis thaliana, AHK5 integrates abiotic and biotic stimuli in stomatal guard cells through regulation of H2O2 homeostasis. Role for AHK5 in the regulation of survival following challenge by a hemi-biotrophic bacterium and a necrotrophic fungus, as well as in the growth response to salt stress. AHK5 positively regulates salt sensitivity and contributes to resistance to the bacterium Pseudomonas syringae pv. tomato DC3000 and the fungal pathogen Botrytis cinerea, detailed overview. Function of AHK5 in regulating the production of hormones and redox homeostasis. Enzyme AHK5 functions as a negative regulator of root growth inhibition mediated by abscisic acid/ethylene. AHK5 positively regulates salt-induced root growth inhibition
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physiological function
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cytokinin signaling is mediated by a multiple-step phosphorelay. Key components of the phosphorelay consist of the histidine kinase (HK)-type receptors, histidine phosphotransfer proteins (HP), and response regulators (RRs). Histidine kinase CKI1 acts upstream of histidine phosphotransfer proteins to regulate female gametophyte development and vegetative growth, role of AHP proteins in female gametophyte development, overview
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physiological function
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Arabidopsis thaliana endosperm formation requires the cytokinin independent 1 (CKI1) histidine kinase, an activator of the cytokinin signaling pathway, which specifies central cells and restricts egg cell fate. Seeds of flowering plants contain embryos and nutritive endosperm arising from double fertilization of two dimorphic female gametes. The key to specification of only one female gamete for endosperm formation is the regulated localization of the CKI1 histidine kinase by expression control and protein translocation. Dimorphism of the two adjacent gametes is mechanistically established in the syncytial embryo sac by spatially restricted CKI1 expression, followed by translocation of endoplasmic reticulum-localized CKI1 protein via nuclear migration. CKI1-directed specification of the endosperm precursor central cell results in seeds containing an embryo and an endosperm, mechanism, overview
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physiological function
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LOV histidine kinase positively regulates the general stress response system and affects the virB operon expression in Brucella abortus. The Brucella genome encodes a sensor histidine kinase containing a LOV domain upstream from the kinase, LOVHK, which plays an important role in light-regulated Brucella virulence. The intracellular signaling pathway is initiated by the light sensor LOVHK, which functionally interacts with two response regulators: PhyR and LovR, constituting a functional two-component signal-transduction system. LOVHK contributes to the activation of the general stress response (GSR) system in Brucella via PhyR, the main regulator of the general stress response system, while LovR is proposed to be a phosphate-sink for LOVHK, decreasing its phosphorylation state. LOVHK plays a role in the intracellular survival of Brucella and in defense of stress induced by starvation. LOVHK signaling cascade, overview
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physiological function
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histidine kinase Chk1p HK is part of a functionally similar but parallel pathway to the Sho1p-Cek1p pathway that confers resistance to the cell wall inhibitors Congo red and calcofluor white
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physiological function
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NikA is responsible for the responses to fungicides such as iprodione and fludioxonil, NikA functions as sensor upstream of the response regulators SskA and SrrA in response to fungicides
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physiological function
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isoform NikA is required for wild-type-like growth on Czapek-Dox medium and a normal resistance to certain oxidative stressors. A NikA mutant grows well in the presence of 1 microg/ml fludioxonil, whereas the wild-type strain is severely impaired in growth. In the presence of fludioxonil, the NikA mutant forms fluffy and often white colonies. Resting conidia of the NikA mutant retain their viability during storage at 4°C
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physiological function
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the FimA-related gene cluster (the fim gene cluster) is positively regulated by the FimS-FimR two-component system. The assembly of mature FimA by a primary structure-dependent mechanism. FimSR is the unique and universal regulatory system that activates the fim gene cluster in a fimA genotype-independent manner
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physiological function
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the TorS histidine kinase activates the trimethylamine-N-oxide reductase pathway when sensing trimethylamine-N-oxide in the environment
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physiological function
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one of the main components of two-component systems, TCSs, is a sensor histidine kinase, which relays extracellular signals to intracellular pathways. VicK is an important sensor histidine kinase in the tooth decay pathogen Streptomyces mutans
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physiological function
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the DraR/DraK two-component system is involved in the differential regulation of antibiotic biosynthesis in a medium-dependent manner, the DraR/DraK two-component system plays an important role in the pH regulation of Streptomyces coelicolor growth medium. The enzyme and the DraR/DraK two-component system are essential for the recovery of the pH of Streptomyces coelicolor growth medium after acid shock, overview
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physiological function
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TcsC is required for wild-type-like growth on Czapek-Dox medium and a normal resistance to certain oxidative stressors. An increased resistance to the cell wall disturbing agents Congo red and Calcofluor white is found for the TcsC mutant
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physiological function
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a GacS mutant devoid of the periplasmic detector domain is severely defective in biofilm formation accompanied by concomitant changes in the expression of small RNAs RsmY/Z that control activation of GacA-regulated genes. Point mutations in a putative ligand binding pocket lined by positively-charged residues originating primarily from the major loop impair biofilm formation
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physiological function
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role of a sensor histidine kinase ChiS as an regulator in pathogenesis. The enzyme regulates the chitin utilization pathway and the associated two required factors, chitin binding protein and chitinases, like ChiA2. Enzyme ChiS is important for adherence and survival in HT-29 cells. ChiS is an important factor for utilizing mucin as a sole nutrient source. Cell adhesion, motility, and mucin penetration depends on ChiS. ChiS affects suckling mice colonization in mice and contributes in fluid accumulation as well as colonization in rabbit intestine
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physiological function
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DraK is a sensory histidine kinase involved in the differential regulation of antibiotics in Streptomyces coelicolor through the DraR/DraK two-component system
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physiological function
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gene VF_A0360 encodes the biofilm inhibitor kinase binK, an orphan hybrid histidine kinase that negatively regulates the Vibrio fischeri symbiotic biofilm (Syp) in vivo and in vitro. Colonization of Euprymna scolopes bobtail squid by Vibrio fischeri bacteria requires bacterial aggregation in host mucus as the symbiont transitions from a planktonic lifestyle in seawater to a biofilm-associated state in the host. Enzyme BinK acts upstream of SypG, the sigma54-dependent transcriptional regulator of the syp biofilm locus. The BinK effects are dependent on intact signaling in the RscS-Syp biofilm pathway. Enzyme BinK antagonizes the signal from RscS and serves as an integral component in Vibrio fischeri biofilm regulation. The hybrid histidine kinase BinK is a negative regulator of in vivo aggregation and squid colonization and of Syp biofilm phenotypes in culture. BinK is acting through SypG and not SypE
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physiological function
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two-component histidine kinases (HKs) regulate responses to environmental stimuli in bacteria and eukaryotes, including yeasts, plants, slime moulds and filamentous fungi. Fungal histidine kinases are involved in osmotic and oxidative stress responses, hyphal development, fungicide sensitivity and virulence. The two-component histidine kinase Shk1 controls stress response, sclerotial formation and fungicide resistance in Sclerotinia sclerotiorum. The expression of SsHOG1 (the last kinase of the Hog pathway) and glycerol accumulation are regulated by the Shk1 gene, but PAK (p21-activated kinase) is not
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physiological function
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two-component signaling pathways are based on phosphoryl group transfer between histidine kinase and response regulator proteins and regulate environmental responses. The DCC-1 protein in Neurospora crasse protein participates in the regulation of processes such as conidiation, perithecial development, and, to a certain degree, carotenogenesis. DCC-1 exerts its effect by promoting cyclic AMP production, including GNA-3 and CR-1, thereby placing this protein within the context of a signaling pathway that operates during conidiation and sexual development. The DCC-1 histidine kinase is required for proper perithecial development, it has a significant role as a negative regulator of sporulation during vegetative growth
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physiological function
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AaHSK1 is a primary regulator for cellular resistance to sugar osmotic stress and for sensitivity to dicarboximide or phenylpyrrole fungicides. Important role of AaHSK1 in osmotic adaption, specifically to sugar osmoticants. AaHSK1 does not play an essential role in fungal pathogenicity
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physiological function
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Ti plasmid-encoded two-component signaling system, designated VirA and VirG, where VirA serves as the histidine autokinase antenna that phosphorylates VirG as the active transcriptional regulator. Histidine kinase VirA processes multiple small molecule host signals (phenol and sugar) and is essential for pathogenesis of Rhizobium radiobacter. A single residue can switch enzyme VirA from a functional AND logic gate to an OR gate where each of two signals activate independently. Host range preferences among natural strains of Rhizobium radiobacter correlate with these gate logic strategies. VirA, which exists in the inner membrane as a homodimer, is composed of multiple domains assigned as periplasmic (P), linker (L), kinase (K), and receiver (R). Sugar perception requires the P domain, whereas phenols require the L domain, localizing detection of these small molecules to opposite sides of the inner membrane. Importance of the integration node, specifically residue 293, as critical for signaling. In most natural isolates, including the frequently used A6 and C58 strains, the wild-type residue for 293 is tyrosine, but in strains Ag162, AB2/73, and KU12, the residue at 293 is phenylalanine. Strains A6, C58, and KU12 are wide-host-range pathogens, whereas strains Ag162 and AB2/73 show limited host ranges
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physiological function
-
a CPR0195 null mutant makes 1000fold fewer spores than its wild-type parent and produces no detectable enterotoxin. CPR0195 functions early during sporulation, i.e., prior to production of sporulation-associated sigma factors. The CPR0195 kinase domain can autophosphorylate and phosphorylate Spo0A
-
additional information
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the coordination and oxidation state of the sensor domain heme iron profoundly affect the enzyme's catalytic activity because they modulate its ATP binding affinity and thus change its kcat/Km(ATP) value. Effects of the response regulator and different divalent metal cations on the autophosphorylation reaction, overview
additional information
the periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize. For NMR structure analysis, the enzyme is prepared with Ag+, Ni2+, Zn2+, and Cu+ ions via dialysis
additional information
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the periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize. For NMR structure analysis, the enzyme is prepared with Ag+, Ni2+, Zn2+, and Cu+ ions via dialysis
additional information
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basic architecture of VirA/VirG histidine kinase: the membrane-embedded VirA histidine kinase contains four modular domains, and the signal inputs activate the VirG response regulator. The sugar-binding protein ChvE interacts with the periplasmic domain, and phenols interact with the linker domain. The linker is predicted to adopt a GAF fold with the alpha1 helix. The conserved His474 is located in the dimerization domain of the kinase
additional information
Hik2 contains a GAF (cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA) domain in the signal input region
additional information
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Hik2 contains a GAF (cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA) domain in the signal input region
additional information
KinD is located upstream of Spo0A and AbrB in the pathway. CACHE is present in many bacterial sensory histidine kinases and is capable of sensing small molecules, often in the presence of cofactors, such as metal ions
additional information
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KinD is located upstream of Spo0A and AbrB in the pathway. CACHE is present in many bacterial sensory histidine kinases and is capable of sensing small molecules, often in the presence of cofactors, such as metal ions
additional information
EvgS is a hybrid histidine kinase composed of a histidine kinase domain, receiver domain, and Hpt transmitter domain. The phosphate at the initial histidine residue in the histidine kinase domain is subsequently transferred to an aspartate residue in the receiver domain and is relayed to the second histidine residue in the Hpt domain before being transferred to the aspartate residue in EvgA
additional information
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EvgS is a hybrid histidine kinase composed of a histidine kinase domain, receiver domain, and Hpt transmitter domain. The phosphate at the initial histidine residue in the histidine kinase domain is subsequently transferred to an aspartate residue in the receiver domain and is relayed to the second histidine residue in the Hpt domain before being transferred to the aspartate residue in EvgA
additional information
-
the HK domain is a monomer in solution and presents autokinase activity
additional information
-
the N-terminal transmembrane domain is dispensable but the PAS domain is needed for the kinase activity
additional information
-
structure-function analysis histidine kinase AHK5 bound to its cognate phosphotransfer protein AHP1, overview. AHP1 binds AHK5RD via a prominent hydrogen bond docking ridge and a hydrophobic patch. AHK5RD binds to AHP1-3 with similar, micromolar affinity, consistent with the transient nature of this signaling complex. Architecture of the AHK5RD-AHP1 Interface, overview
additional information
the VicK kinase activates itself by helical bending of the DHp domain and coordinated swinging around of the catalytic and ATP binding domain to engage with the target histidine. Modelling of the active state structure of the catalytic ATP-binding domain and positioning of inactive domain. Structure-function analysis of the enzyme domains, detailed overview. Transient formation of the active site
additional information
effect of the nonconserved flanking sequence on the signaling lifetime of LovK, the effects of structure outside the LOV core on its signaling lifetime do not combine in a simple, additive way. Kinetics of recovery from the adduct state depend not only on the buffer environment but also on the structural context in which the LOV domain is contained. Full-length LovK (residues 1-368) has a long recovery, with a half-life of 2 h, the isolated LOV core (residues 25-138) recovers more quickly, with a half-life of 37 min. LovK (25-163), which contains the LOV core and the nonconserved linker sequence at its C-terminus, has a recovery half-life of 28 min. A construct containing the LOV core and the nonconserved N-terminal flanking sequence, LovK(1-138), has a half-life of only 2 min, but this N-terminal region has not a general rate enhancement effect. LovK(1-163), a construct with fully intact N- and C-termini (but missing the kinase domain), is slower to recover than either LovK(25-138), LovK(1-138), or LovK(25-163)
additional information
-
effect of the nonconserved flanking sequence on the signaling lifetime of LovK, the effects of structure outside the LOV core on its signaling lifetime do not combine in a simple, additive way. Kinetics of recovery from the adduct state depend not only on the buffer environment but also on the structural context in which the LOV domain is contained. Full-length LovK (residues 1-368) has a long recovery, with a half-life of 2 h, the isolated LOV core (residues 25-138) recovers more quickly, with a half-life of 37 min. LovK (25-163), which contains the LOV core and the nonconserved linker sequence at its C-terminus, has a recovery half-life of 28 min. A construct containing the LOV core and the nonconserved N-terminal flanking sequence, LovK(1-138), has a half-life of only 2 min, but this N-terminal region has not a general rate enhancement effect. LovK(1-163), a construct with fully intact N- and C-termini (but missing the kinase domain), is slower to recover than either LovK(25-138), LovK(1-138), or LovK(25-163)
additional information
protein-protein docking analysis of the catalytic domain with the dimerization DHp domain of DesK, the C-terminal part of the ATP lid interacts with helix alpha1 of the DHp, through hydrogen bonds between His335 and Asp289 as well as Gly199 with Lys333, overview
additional information
-
protein-protein docking analysis of the catalytic domain with the dimerization DHp domain of DesK, the C-terminal part of the ATP lid interacts with helix alpha1 of the DHp, through hydrogen bonds between His335 and Asp289 as well as Gly199 with Lys333, overview
additional information
conserved proline-222, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. The proline is essential for phosphatase activity. The C-terminal ends of the VicK dimer harbor two monomeric catalytic domains. The enzyme architecture with a signal transducer and sensor domain suggests a model where DHp helical bending and a CA swing movement are likely coordinated for autokinase activation, structure-function analysis, overview
additional information
mechanism for the pH-dependent conformational change of the extracellular sensor domain of DraK protein involving residues E83, E105, and E107 with very high pKa values, overview
additional information
-
mechanism for the pH-dependent conformational change of the extracellular sensor domain of DraK protein involving residues E83, E105, and E107 with very high pKa values, overview
additional information
LOV domains are blue-light sensory modules which bind a flavin molecule as cofactor
additional information
-
LOV domains are blue-light sensory modules which bind a flavin molecule as cofactor
additional information
-
KinD is located upstream of Spo0A and AbrB in the pathway. CACHE is present in many bacterial sensory histidine kinases and is capable of sensing small molecules, often in the presence of cofactors, such as metal ions
-
additional information
-
protein-protein docking analysis of the catalytic domain with the dimerization DHp domain of DesK, the C-terminal part of the ATP lid interacts with helix alpha1 of the DHp, through hydrogen bonds between His335 and Asp289 as well as Gly199 with Lys333, overview
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additional information
-
the N-terminal transmembrane domain is dispensable but the PAS domain is needed for the kinase activity
-
additional information
-
LOV domains are blue-light sensory modules which bind a flavin molecule as cofactor
-
additional information
-
the VicK kinase activates itself by helical bending of the DHp domain and coordinated swinging around of the catalytic and ATP binding domain to engage with the target histidine. Modelling of the active state structure of the catalytic ATP-binding domain and positioning of inactive domain. Structure-function analysis of the enzyme domains, detailed overview. Transient formation of the active site
-
additional information
-
mechanism for the pH-dependent conformational change of the extracellular sensor domain of DraK protein involving residues E83, E105, and E107 with very high pKa values, overview
-
additional information
-
conserved proline-222, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. The proline is essential for phosphatase activity. The C-terminal ends of the VicK dimer harbor two monomeric catalytic domains. The enzyme architecture with a signal transducer and sensor domain suggests a model where DHp helical bending and a CA swing movement are likely coordinated for autokinase activation, structure-function analysis, overview
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additional information
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basic architecture of VirA/VirG histidine kinase: the membrane-embedded VirA histidine kinase contains four modular domains, and the signal inputs activate the VirG response regulator. The sugar-binding protein ChvE interacts with the periplasmic domain, and phenols interact with the linker domain. The linker is predicted to adopt a GAF fold with the alpha1 helix. The conserved His474 is located in the dimerization domain of the kinase
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Show AA Sequence and Transmembrane Helices (721850 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46000
-
YbdK-transmembrane domain dodecyl-phosphocholine complex, solution state NMR T1/T2 relaxation analysis
50000
75000
83000
99000
additional information
additional information
CusSs samples for analytical ultracentrifugation experiments are prepared by dialysis against 5fold molar excesses of AgNO3, ZnCl2 or NiCl2
additional information
-
CusSs samples for analytical ultracentrifugation experiments are prepared by dialysis against 5fold molar excesses of AgNO3, ZnCl2 or NiCl2
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotetramer
monomer
oligomer
tetramer
and monomer and oligomer, 4 * 48500, calculated from sequence, 4 * 50000, SDS-PAGE.The functional form of Hik2 is a higher-order oligomer such as a hexamer or octamer
additional information
dimer
-
the Brucella HK domain presents two different dimeric assemblies in the asymmetric unit: one similar to canonical parallel homodimers (C) and the other, an antiparallel non-canonical (NC) dimer, each with distinct relative subdomain orientations and dimerization interfaces. The C dimer is the functionally relevant species and can be stabilized and is active in solution. The HK domain is a monomer in solution and presents autokinase activity
dimer
the overall structure of Ag(I)-CusS(39-187) is a mixed alpha/beta fold with a PAS-like topology. The central five-stranded anti-parallel beta-sheet is flanked by alpha-helices on either side. The structure begins with a long N-terminal alpha-helix and ends with a short C-terminal alpha-helix that both lie on the same side of the sheet, The structure of the periplasmic sensor domain of the histidine kinase CusS shows unusual metal ion coordination at the dimeric interface, enzyme CusS forms a homodimer with four Ag(I) binding sites per dimeric complex. Metal-induced dimerization results in increases in kinase activity in the cytoplasmic domains of CusS. There are four Ag(I)-CusS(39-187) molecules in the asymmetric unit that interact to form two homodimers
dimer
periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize
dimer
-
the signal transduction histidine kinase domain, H-NOXA revealing a Per-Arnt-Sim fold, monomers dimerize in a parallel arrangement juxtaposing their N-terminal helices and preceding residues, overview
dimer
dimeric PaBphP-PCD structure with PAS, GAF, and PHY domains, interdomain and histidine kinase domain, domain structure, overview
dimer
-
AgrC forms ligand-independent dimers that undergo trans-autophosphorylation upon interaction with autoinducing peptide
dimer
the extracellular domain of enzyme YycG exhibits two dimerization modes, dimerization configurations, cross-linking experiments, overview. Both YycH and YycI are required to inhibit the dimerization of YycG
dimer
-
the extracellular domain of enzyme YycG exhibits two dimerization modes, dimerization configurations, cross-linking experiments, overview. Both YycH and YycI are required to inhibit the dimerization of YycG
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dimer
the dimeric VicK protein has a rod-shaped structure with the domains linearly connected like beads on a string
dimer
-
the dimeric VicK protein has a rod-shaped structure with the domains linearly connected like beads on a string
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dimer
the holoenzyme exists as a stable dimer in solution. The overall structure of VicK is a long-rod dimer that anchors four connected domains: HAMP, Per-ARNT-SIM (PAS), DHp, and catalytic and ATP binding domain (CA). The HAMP, a signal transducer, and the PAS domain, major sensor, adopt canonical folds with dyad symmetry. In contrast, the dimer of the DHp and CA domains is asymmetric because of different helical bends in the DHp domain and spatial positions of the CA domains. A conserved proline, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. Following the transmembrane domain, the HAMP signal transducer domain and PAS sensor domain are directly connected to the catalytic domain through a DHp domain, a dimerization and histidine phosphorylation domain. Structure of the HAMP domain (aa 36-86), located at the uppermost position within the N-terminal region of the VicK structure, overview
dimer
-
the holoenzyme exists as a stable dimer in solution. The overall structure of VicK is a long-rod dimer that anchors four connected domains: HAMP, Per-ARNT-SIM (PAS), DHp, and catalytic and ATP binding domain (CA). The HAMP, a signal transducer, and the PAS domain, major sensor, adopt canonical folds with dyad symmetry. In contrast, the dimer of the DHp and CA domains is asymmetric because of different helical bends in the DHp domain and spatial positions of the CA domains. A conserved proline, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. Following the transmembrane domain, the HAMP signal transducer domain and PAS sensor domain are directly connected to the catalytic domain through a DHp domain, a dimerization and histidine phosphorylation domain. Structure of the HAMP domain (aa 36-86), located at the uppermost position within the N-terminal region of the VicK structure, overview
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homodimer
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YbdK-transmembrane domain forms homodimers in dodecyl-phosphocholine micelles, cross-linking assay and analytical ultracentrifugation analysis
homodimer
histidine kinases are composed of an N-terminal sensory (or input) domain, which senses external stimuli, and a conserved kinase domain, which contains an N-terminal dimerization and histidine phosphotransfer domain and a catalytic and ATP binding (CA) domain
homotetramer
-
KinC becomes active by forming a homotetramer via the N-terminal PAS domain
homotetramer
-
KinC becomes active by forming a homotetramer via the N-terminal PAS domain
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monomer
and tetramer and oligomer, 1 * 48500, calculated from sequence, 1 * 50000, SDS-PAGE.The functional form of Hik2 is a higher-order oligomer such as a hexamer or octamer
oligomer
intact YycG HK can form higher-order oligomers at the cell membrane via combinations of the H- and L-dimeric interacting surfaces
oligomer
-
intact YycG HK can form higher-order oligomers at the cell membrane via combinations of the H- and L-dimeric interacting surfaces
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oligomer
and tetramer and monomer, x * 48500, calculated from sequence, x * 50000, SDS-PAGE.The functional form of Hik2 is a higher-order oligomer such as a hexamer or octamer
additional information
-
basic architecture of VirA/VirG histidine kinase: the membrane-embedded VirA histidine kinase contains four modular domains, and the signal inputs activate the VirG response regulator. The sugar-binding protein ChvE interacts with the periplasmic domain, and phenols interact with the linker domain. The linker is predicted to adopt a GAF fold with the alpha1 helix. The conserved His474 is located in the dimerization domain of the kinase
additional information
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basic architecture of VirA/VirG histidine kinase: the membrane-embedded VirA histidine kinase contains four modular domains, and the signal inputs activate the VirG response regulator. The sugar-binding protein ChvE interacts with the periplasmic domain, and phenols interact with the linker domain. The linker is predicted to adopt a GAF fold with the alpha1 helix. The conserved His474 is located in the dimerization domain of the kinase
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additional information
the enzyme AaHSK1 has several conserved domains and motifs, such as a HAMP (histidine kinase, adenylate cyclase, methyl binding protein, and phosphatase) domain and a dimerization/phosphoacceptor domain. AaHSK1 contains four repeat domains within HAMP
additional information
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the enzyme AaHSK1 has several conserved domains and motifs, such as a HAMP (histidine kinase, adenylate cyclase, methyl binding protein, and phosphatase) domain and a dimerization/phosphoacceptor domain. AaHSK1 contains four repeat domains within HAMP
additional information
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the enzyme AaHSK1 has several conserved domains and motifs, such as a HAMP (histidine kinase, adenylate cyclase, methyl binding protein, and phosphatase) domain and a dimerization/phosphoacceptor domain. AaHSK1 contains four repeat domains within HAMP
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additional information
high affinity binding is observed between AHK1 monomers resulting in the formation of the dimer present at physiological conditions. A high affinity interaction is also observed between AHK1 and AHP2 transfer protein
additional information
determination of the importance of several residues at the dimer interface for KinA enzymatic activity in vitro and in vivo, KinA architecture and domain structure, and PAS-A domain organization and secondary structure, overview
additional information
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determination of the importance of several residues at the dimer interface for KinA enzymatic activity in vitro and in vivo, KinA architecture and domain structure, and PAS-A domain organization and secondary structure, overview
additional information
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the N-terminal transmembrane domain is dispensable but the PAS domain is needed for the kinase activity
additional information
analysis of the structure of enzyme catalytic and ATP-binding domain using the crystal structure, overview
additional information
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analysis of the structure of enzyme catalytic and ATP-binding domain using the crystal structure, overview
additional information
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determination of the importance of several residues at the dimer interface for KinA enzymatic activity in vitro and in vivo, KinA architecture and domain structure, and PAS-A domain organization and secondary structure, overview
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additional information
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analysis of the structure of enzyme catalytic and ATP-binding domain using the crystal structure, overview
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additional information
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the N-terminal transmembrane domain is dispensable but the PAS domain is needed for the kinase activity
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additional information
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Brucella LOV-HK comprises an N-terminal blue-light sensor (LOV) domain, followed by a central PAS domain and a C-terminal HK domain. Crystal structure analysis, overview
additional information
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the N-terminus of HK17 forms a GAF domain, structure of the RR-HK17 two-component system
additional information
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the periplasmic region of histidine kinase EnvZ(Ala38-Arg162) forms a dimer in solution
additional information
NMR structure analysis, localization and structural model, detailed overview
additional information
CusS is predicted to be a canonical histidine kinase with a periplasmic sensor domain connected by transmembrane helices to the catalytic cytoplasmic domains
additional information
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CusS is predicted to be a canonical histidine kinase with a periplasmic sensor domain connected by transmembrane helices to the catalytic cytoplasmic domains
additional information
EvgS is a hybrid histidine kinase composed of a histidine kinase domain, receiver domain, and Hpt transmitter domain. EvgS has a large periplasmic sensor region consisting of two tandem bacterial periplasmic solute-binding protein (PBPb) domains at its N-terminus. The periplasmic sensor region of EvgS is necessary for EvgS activation, and Leu152, located within the first PBPb domain, is involved in the activation. Alkali metals are perceived at the periplasmic sensor region, whereas the cytoplasmic linker domain, connecting the transmembrane region and the histidine kinase domain, is required for low-pH perception
additional information
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EvgS is a hybrid histidine kinase composed of a histidine kinase domain, receiver domain, and Hpt transmitter domain. EvgS has a large periplasmic sensor region consisting of two tandem bacterial periplasmic solute-binding protein (PBPb) domains at its N-terminus. The periplasmic sensor region of EvgS is necessary for EvgS activation, and Leu152, located within the first PBPb domain, is involved in the activation. Alkali metals are perceived at the periplasmic sensor region, whereas the cytoplasmic linker domain, connecting the transmembrane region and the histidine kinase domain, is required for low-pH perception
additional information
DcuS shows a mixed alpha/beta-structure containing two subdomains of similar folds, each consisting of a five-stranded antiparallel beta-sheet flanked by helices on either side, structure analysis, residues 42-181 comprise the sensory domain of the enzyme, dimerization of DcuS-42181, overview
additional information
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the N-terminal domain in an STHK from Nostoc punctiforme is homologous to the central region in soluble guanylyl cyclase, the main receptor for nitric oxide, structure-function analysis and dimerization mechanism, overview
additional information
modeling of the full-length bacteriophytochrome structure, including its output histidine kinase domain, structure-function relationship, overview
additional information
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modeling of the full-length bacteriophytochrome structure, including its output histidine kinase domain, structure-function relationship, overview
additional information
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Ppr is composed of three domains, a PYP domain, a bacteriophytochrome Bph domain, and a histidine kinase domain, in the order from the N- to the C-terminal of Ppr
additional information
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Both YycH and YycI are required to inhibit the dimerization of YycG. Genes yycH and yycI are members of the yyc operon. The actions of YycH and YycI on YycG likely occur at the transmembrane helices, in which an octameric complex was formed by an YycG homodimer flanked by YycH-YycI heterodimers
additional information
Both YycH and YycI are required to inhibit the dimerization of YycG. Genes yycH and yycI are members of the yyc operon. The actions of YycH and YycI on YycG likely occur at the transmembrane helices, in which an octameric complex was formed by an YycG homodimer flanked by YycH-YycI heterodimers
additional information
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Both YycH and YycI are required to inhibit the dimerization of YycG. Genes yycH and yycI are members of the yyc operon. The actions of YycH and YycI on YycG likely occur at the transmembrane helices, in which an octameric complex was formed by an YycG homodimer flanked by YycH-YycI heterodimers
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additional information
enzyme VicK is composed of several domains (HAMP, PAS, DHp, and catalytic and ATP binding domain [CA]) in addition to a short transmembrane domain. Domain structure-function relationship and analysis, overview. The overall structure of VicK comprises a dimer in the shape of a long slim rod
additional information
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enzyme VicK is composed of several domains (HAMP, PAS, DHp, and catalytic and ATP binding domain [CA]) in addition to a short transmembrane domain. Domain structure-function relationship and analysis, overview. The overall structure of VicK comprises a dimer in the shape of a long slim rod
-
additional information
enzyme DraK consists of an extracellular domain flanked by two transmembrane helices (Leu5-Val27 and Leu126-Ile145), a sensory domain (Glu28-Thr125), a HAMP (histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins and phosphatases) domain (Asn149-Thr201) and a kinase domain (Ala202-Pro410) composed of His KA and CA domains
additional information
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enzyme DraK consists of an extracellular domain flanked by two transmembrane helices (Leu5-Val27 and Leu126-Ile145), a sensory domain (Glu28-Thr125), a HAMP (histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins and phosphatases) domain (Asn149-Thr201) and a kinase domain (Ala202-Pro410) composed of His KA and CA domains
additional information
monomer-dimer equilibrium of the shortened extracellular sensing domain of DraK in solution, with MWs of 9.7 kDa for the monomeric and 19.4 kDa for the dimeric form
additional information
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monomer-dimer equilibrium of the shortened extracellular sensing domain of DraK in solution, with MWs of 9.7 kDa for the monomeric and 19.4 kDa for the dimeric form
additional information
mechanism for the pH-dependent conformational change of the the extracellular sensor domain protein of DraK, overview. The structure contains a mixed alpha-beta fold, adopting a fold similar to the ubiquitous sensor domain of histidine kinase
additional information
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mechanism for the pH-dependent conformational change of the the extracellular sensor domain protein of DraK, overview. The structure contains a mixed alpha-beta fold, adopting a fold similar to the ubiquitous sensor domain of histidine kinase
additional information
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mechanism for the pH-dependent conformational change of the the extracellular sensor domain protein of DraK, overview. The structure contains a mixed alpha-beta fold, adopting a fold similar to the ubiquitous sensor domain of histidine kinase
-
additional information
-
enzyme DraK consists of an extracellular domain flanked by two transmembrane helices (Leu5-Val27 and Leu126-Ile145), a sensory domain (Glu28-Thr125), a HAMP (histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins and phosphatases) domain (Asn149-Thr201) and a kinase domain (Ala202-Pro410) composed of His KA and CA domains
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additional information
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Hik33 has several subdomains in its N-terminal region, two of which are transmembrane (TM) helices (TM1 and TM2), and it is located on plasma and/or thylakoid membranes. The N-terminal region also includes a periplasmic loop region between the TM helices, a HAMP domain, and a PAS domain. Analysis of the enzyme subdomains of the N-terminal region
additional information
Hik33 has several subdomains in its N-terminal region, two of which are transmembrane (TM) helices (TM1 and TM2), and it is located on plasma and/or thylakoid membranes. The N-terminal region also includes a periplasmic loop region between the TM helices, a HAMP domain, and a PAS domain. Analysis of the enzyme subdomains of the N-terminal region
additional information
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analysis of the enzyme subdomains of the N-terminal region
additional information
analysis of the enzyme subdomains of the N-terminal region
additional information
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DctB shows a mixed alpha/beta-structure containing two subdomains of similar folds, each consisting of a five-stranded antiparallel beta-sheet flanked by helices on either side, structure analysis, residues 28-286 comprise the sensory domain of the enzyme, overview
additional information
Vibrio cholerae serotype O1 MO45
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DctB shows a mixed alpha/beta-structure containing two subdomains of similar folds, each consisting of a five-stranded antiparallel beta-sheet flanked by helices on either side, structure analysis, residues 28-286 comprise the sensory domain of the enzyme, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no phosphoprotein
no automodification of AHK1 with ATP is observed
phosphoprotein
additional information
phosphoprotein
BA2291 performs GTP-dependent autophosphorylation
phosphoprotein
-
BA2291 performs GTP-dependent autophosphorylation
-
phosphoprotein
activation of LOVHK by blue-light increases the autophosphorylation activity of the HK domain of the histidine kinase
phosphoprotein
-
activation of LOVHK by blue-light increases the autophosphorylation activity of the HK domain of the histidine kinase
-
phosphoprotein
-
phosphorylation of CckA is required for function but is not important for polar localization
phosphoprotein
-
the enzyme HK17 performs autophosphorylation stimulated by ethanolamine
phosphoprotein
enzyme undergoes phosphorylation in the presence of ATP
phosphoprotein
the major site at which NRII is autophosphorylated is contained within a peptide consisting of amino acid residues 136-142 of NRII, and thus probably corresponds to H139. A minor site of phosphorylation, accounting for about 2% of the phosphate in NRII-P, is found in a peptide that corresponds to residues 158-169
phosphoprotein
the phosphotransfer domain, CheA1-134, contains the site of phosphorylation, His48, and two other histidine residues, His26 and His67
phosphoprotein
His243 is the a site of autophosphorylation as well as transphosphorylation to the conserved D55 residue of response regulator OmpR
phosphoprotein
purified BarA protein is able to autophosphorylate when incubated with [gamma-(32)P]ATP but not with [alpha-(32)P]ATP or [gamma-(32)P]GTP. Phosphorylated BarA, in turn, acts as an efficient phosphoryl group donor to UvrY. BarA and UvrY constitute a new two-component system for gene regulation in Escherichia coli
phosphoprotein
-
autophosphorylation, histidine-398 in the conserved H-box is the phospho-accepting site
phosphoprotein
ATP-dependent autophosphorylation occurs at a conserved His residue in the kinase core. The phosphoryl group is then transferred from the histidine kinase to a conserved Asp residue on the N-terminal receiver domain of the response regulator, which in turn activates the C-terminal effector domain to mediate an adaptive response. The phosphorylated response regulator activates transcription of genes that respond to the environmental stimulus
phosphoprotein
-
autophosphorylation of the homodimer occurs in trans. No cooperativity in autophosphorylation of CpxA is observed despite its asymmetric structures. Minor amounts of ADP generated during autophosphorylation reactions or present in ATP preparations, can produce about 50% total phosphorylation
phosphoprotein
-
low pH triggers the autophosphorylation of the histidine kinase ArsS
phosphoprotein
the enzyme autophosphorylates in vitro on the conserved histidine residue and then transfers the phosphoryl group to the conserved aspartate residue in the associated receiver domain
phosphoprotein
MHZ1 is autophosphorylated at a conserved histidine residue
phosphoprotein
in the presence of [gamma-32P]ATP, the purified COOH-terminal KinB protein undergoes progressive autophosphorylation in vitro. Substitutions of the residues conserved among histidine protein kinases abolishes KinB autophosphorylation
phosphoprotein
-
histidine kinases autophosphorylate prior to transferring the phosphate to a response regulator
phosphoprotein
-
AgrC forms ligand-independent dimers that undergo trans-autophosphorylation upon interaction with autoinducing peptide
phosphoprotein
-
the Slr1759 histidine kinase domain undergoes autophosphorylation in vitro
phosphoprotein
Hik2 undergoes autophosphorylation on a conserved histidine residue, at pH 7.5 and 22°C, and becomes rapidly dephosphorylated by the action of response regulators Rre1 and RppA (regulator of phycobilisome association), at pH 7.5 and 30°C. The autophosphorylation of Hik2 is specifically inhibited by sodium ions
additional information
-
the enzyme performs regulatory autophosphorylation
additional information
in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase
additional information
in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase
additional information
-
in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 2.54 M ammonium sulfate, 15.9% (v/v) glycerol, and 0.1 M MES buffer pH 5.05
-
puriifed kinase AHK5RD in complex with AHP1, X-ray diffraction structure determination and analysis at 1.95 A resolution
-
structures of free, Mg2+-bound, and beryllofluoridated CKI1RD (a stable analogue of the labile phosphorylated form) are identical and similar to the active state of receiver domains of bacterial response regulator. Mg2+ binding and beryllofluoridation alter the conformational equilibrium of the beta3-alpha3 loop close to the phosphorylation site. Mutations that perturbe the conformational behavior of the beta3-alpha3 loop while keeping the active-site aspartate intact result in suppression of CKI1 function. The beta3-alpha3 loop may directly interact with the ATP-binding site of the CKI1 histidine kinase domain
purified recombinant DesK mutant H188V catalytic and ATP-binding domain in complex with ATP, by hanging drop vapour diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 300 mM NaCl, 0.5 mM DTT, 10 mM MgCl2, 5 mM ATP, and 5 mM BeF3, with 0.002 ml of reservoir solution containing 20% PEG 3350, 0.2 M NH4ClX-ray diffraction structure determination and analysis at 1.8 A resolution
purified recombinant residues 10-117 of KinA, fused to an N-terminal His6Gbeta1-tag and a TEV protease site in the tag-protein linker, free or as selenomethionine-tagged variant, hanging-drop vapor-diffusion method, 20°C, mixing of 0.001 ml 7 mg/mL protein solution containing 25 mM Tris pH 8.0, 100 mM NaCl, with 0.001 ml well solution containing 13-15% w/v PEG 10000, 0.1 M ammonium acetate, and 0.1 M bis-Tris, pH 5.5, and with 20 mM DTT in case of the selenomethionine-labeled protein, 4 days, cryoprotetion using 25% v/v glycerol, X-ray diffraction structure determination and analysis at 1.7-2.0 A resolution
the phosphorylated cytoplasmic domain of DesK is crystallized by hanging drop vapor diffusion, using 10% (w/v) PEG 3000, 0.1 M CHES, pH 9.5, and 10 mM MgCl2, at 18°C
Brucella LOV-HK histidine kinase domain free or in complex with non-hydrolyzable ATP analogue AMP-PCP, mixing of 1 mg/ml protein in 50 mM MES, pH 6.5, and 250 mM sodium chloride, with precipitation solution, X-ray diffraction structure determination and analysis at 2.51 A resolution, molecular modeling
-
crystal structure at 2.0 A resolution of the complex of the Escherichia coli chemotaxis response regulator CheY and the phosphoacceptor-binding domain P2 of the kinase CheA
crystal structure, at 2.95 A resolution, of the response regulator of bacterial chemotaxis, CheY, bound to the recognition domain from its cognate histidine kinase, CheA
crystallization of a complex between a novel C-terminal transmitter, HPt domain, of the anaerobic sensor kinase ArcB and the chemotaxis response regulator CheY
EvgS has a large periplasmic domain and a cytoplasmic PAS domain in addition to phospho-acceptor, histidine kinase and dimerization, internal receiver, and phosphotransfer domains. Homology modeling of the periplasmic region of EvgS leads to a model in which EvgS senses both external and internal pH and is activated by a shift from a tight inactive to a weak active dimer
free and in complex with nitrate, hanging drop vapor diffusion method, using 0.1 M Tris-HCl (pH 8.5) and 2 M NH4H2PO4 at 4°C (enzyme in complex with nitrate) or using 23% (w/v) polyethylene glycol 3350, 1% (v/v) isopropanol, and 0.1 M HEPES (pH 7.5) at 4°C (free apo-enzyme)
hanging drop vapor diffusion method, at 4°C against a buffer containing 5%10% (v/v) 1-4 butanediol, 0.1 M Na-aetate (pH 5.5), 25100 mM NH4SO4
purified recombinant Ag(I)-bound periplasmic sensor domain, Ag(I)-CusS(39-187), sitting drop vapor diffusion method, mixing of 200 nl of 7-8 mg/ml protein in 25 mM MES, pH 6.0, with 200 nl of precipitant solution containing 100 mM Tris-HCl, pH 8.5, 200 mM ammonium acetate, and 25% PEG 3350, 4°C, equilibration against 1 ml precipitant solution, method optimization, X-ray diffraction structure determination and analysis, single anomalous diffraction (SAD) method at 2.15 A resolution. There are four Ag(I)-CusS(39-187) molecules in the asymmetric unit that interact to form two homodimers
recombinant chimeric protein formed by the EnvZ catalytic domain with the HAMP domain of the Archaeoglobus fulgidus Af1503 receptor, with or without the point mutation A291F, sitting drop vapor diffusion method, mixing of 400 nl of 2 and 20 mg/mlprotein, respectively, in 30 mM MOPS, pH 7.0 and 50 mM NaCl, for the wild-type construct and in a buffer containing 20 mM MOPS, pH 7.0 and 100 mM NaCl for the A291F mutant, with 400 nl of reservoir solution and equilibration against 0.05 mL reservoir solution, containing 0.1 M MMT buffer, pH 4.0, and 25% (w/v) PEG 1500 for the wild-type fusion and 0.2 M lithium acetate and 20% w/v PEG 3350 for the A291F variant, 22°C, X-ray diffraction tructure determination and analysis. The structure shows a putatively active conformation of the catalytic domain, molecular replacement
structures of CpxA trapped as a hemi-phosphorylated dimer, and of the receiver domain from the response regulator partner, CpxR. The autophosphorylation of a histidine residue and the subsequent phosphoryl transfer to its response regulator CpxR can occur simultaneously, one in each protomer of the asymmetric CpxA dimer. The autokinase activity increases in the presence of phosphotransfer-impaired CpxR. In an allosteric switching mechanism, CpxR binding to one CpxA protomer may trigger autophosphorylation in the second protomer
purified recombinant selenomethionine-labeled and wild-type GST-tagged DcuS residues 42-181 in complex with C4-dicarboxylate ligand, 18.5 mg/ml protein, hanging-drop vapor diffusion, using a reservoir buffer containing 20-24% PEG monoethyl ether 2000, 15% isopropyl alcohol, 0.2 M ammonium citrate, and 0.1 M sodium acetate, pH 4.5, at 4 °C, 1 week, X-ray diffraction structure determination and analysis
in complex with inhibitor Sda, crystals only form in the presence of ADP-Mg2+ (but not with ATP or AMPPNP, and not in the absence of nucleotide)
-
hanging drop vapor diffusion method, using 8% (v/v) isopropanol, 2% (w/v) PEG 3350, 150 mM calcium acetate, and 100 mM MES, pH 6.0, at 4°C
citrate-free or citrate-bound CitA, hanging drop vapor diffusion method, using either 0.1 M HEPES, pH 7.5, 1.6 M (NH4)2SO4, and 5 mM sodium citrate or using 20 mM HEPES, pH 7.5, 0.63 M NaH2PO4 and 0.63 M KH2PO4
dimerized signal transduction histidine kinase domain H-NOXA domain residues 8-121, 4°C, sitting-drop vapor diffusion, 20 mg/ml NpSTHK8121 in 5 mM Tris, pH 7.5, 100 mM NaCl, 1 mM 2-mercaptoethanol, is mixed with an equal volume of reservoir solution containing 1.7-1.9 M ammonium sulfate, 100 mM Tris-HCl, pH 7.7-9.0, for crystallization of the full-length enzyme, 15 mg/ml protein is mixed with equal volume of 0.1 M HEPES, pH 7.5, and 1.5 M lithium sulfate monohydrate, crystals appear after 3 days at 20°C, X-ray diffraction structure determination and analysis at 2.1 A resolution
-
crystal structure of the CzcS sensor domain in complex with Zn(II) at 1.7 A resolution. The sensor domain is an alpha/beta-fold and senses the Zn(II) stimulus at micromole level in a tetrahedral geometry through its symmetry-related residues His55 and Asp60 on the dimer interface. The sensor domain interacts with the effector with the N-terminal alpha-helices rather than the conserved beta-sheets pocket. The dimerization of the N-terminal H1 and H1' alpha-helices is of primary importance for the activity of histidine kinase activity
NMR solution structure, the GacS periplasmic domain displays a distinct PDC/PAS alpha/beta fold characterized by a three-stranded beta-sheet flanked by alpha-helices and an atypical major loop
wild-type and mutant bacteriophytochrome with an intact, fully photoactive photosensory core domain in its darkadapted Pfr state, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement
structure of the cytoplasmic PAS domain, residues valine 251 to arginine 376. The metal-binding site comprises a single Zn2+ ion bound by the atoms Ndelta1 from His271, Odelta1 from Asp274, Ndelta1 from His364 and Oepsilon2 from Glu368 in a slightly distorted tetrahedral coordination geometry
complete cytoplasmic region of enzyme VicK, X-ray diffraction structure determination and analysis
purified full-length enzyme, X-ray diffraction structure determination and analysis at 3 A resolution, modeling
purified recombinant N-terminally His6-tagged extracellular sensory domain of DraK, sitting drop vapour diffusion method, mixing 200 nl of of 12 mg/ml protein in 10 mM sodium acetate, pH 4.5, and 100 mM NaCl with reservoir solution containing 0.2 M potassium/sodium tartrate, and 20% PEG 3350, and equilibration against 0.070 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
P3P4 domain structure of Thermotoga maritima CheA, vapor diffusion method, mixing of 0.001 ml of 0.7 mM protein in 50 mM HEPES, pH 7.5, 150 mM NaCl, and 2 mM DTT, with 0.001 ml of reservoir solution containing 0.5 M ammonium sulfate, 0.1 M sodium citrate tribasic dihydrate, pH 5.6, and 1.0 M lithium sulfate monohydrate, 4°C, X-ray small angle diffraction structure determination and analysis at 3.0 A resolution, molecular replacement and modelling
-
ThkA complexed with the response regulator TrrA, by the batch method, X-ray crystallography at a resolution of 4.2 A, 2fold symmetry, two monomeric TrrAs bind to the ThkA dimer
recombinant selenomethionine-labeled DctB residues 28-286 in complex with C4-dicarboxylate ligand, by hanging-drop vapor diffusion at 4°C against a buffer containing 6% isopropyl alcohol, 0.2 M calcium acetate, and 0.1 M Tris-HCl, pH 7.5, the protein concentration is 8.5 mg/ml with a protein to buffer ratio of 1:1, 2 weeks, X-ray diffraction structure determination and analysis
-
hanging drop vapor diffusion method, at 4°C against a buffer containing 7%13% (w/v) PEG 4000, 0.1 M Tris (pH 7.5)
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y293F
-
site-directed mutagenesis, Y293F substitution in full-length VirA changes the phenol perception, mutation VirA(LKR)D280-284,Y293F does not alter phenol specificity nearly to the extent as mutant Y293T, it does increase the activity of virtually all active phenols roughly 30fold above that of VirA(LKR)D280-284. Acetosyringone sensitivity increases in VirAY293F with and without glucose
Y293T
-
site-directed mutagenesis, Y293T substitution in full-length VirA changes the phenol perception, mutation VirA(LKR)D280-284,Y293T alters phenol specificity of the enzyme
Y293F
-
site-directed mutagenesis, Y293F substitution in full-length VirA changes the phenol perception, mutation VirA(LKR)D280-284,Y293F does not alter phenol specificity nearly to the extent as mutant Y293T, it does increase the activity of virtually all active phenols roughly 30fold above that of VirA(LKR)D280-284. Acetosyringone sensitivity increases in VirAY293F with and without glucose
-
Y293T
-
site-directed mutagenesis, Y293T substitution in full-length VirA changes the phenol perception, mutation VirA(LKR)D280-284,Y293T alters phenol specificity of the enzyme
-
D1050A
mutation changes conformation of the beta3-alpha3 loop in solution and shifts residue F1102 to the inactive orientation
D1050E
mutation changes conformation of the beta3-alpha3 loop in solution and shifts residue F1102 to the inactive orientation
S147L
F436S
-
the mutation increases the efficiency of sporulation in cells overexpressing KinA inhibitor Sda by about 10fold while actually reducing the efficiency of sporulation in cells that lack sda
G192C/G334C
site-directed mutagenesis, the Cys-engineered mutant is used for interdomain disulfide covalent bonding studies
H188V
I108A
the point mutation does not affect KinA autophosphorylation activity, but interfers with KinA PAS-A dimerization
I95A
the point mutation slightly reduces the KinA autophosphorylation activity and interfers with KinA PAS-A dimerization
I95E
the point mutation reduces the KinA autophosphorylation activity and interfers with KinA PAS-A dimerization
K32E/E36K
mutations in linker region, mutant shows higher activity at higher pH and maintains pH regulation
P410L
-
the mutation increases the efficiency of sporulation in cells overexpressing KinA inhibitor Sda by about 10fold while actually reducing the efficiency of sporulation in cells that lack sda
Q193C/G334C
site-directed mutagenesis, the Cys-engineered mutant is used for interdomain disulfide covalent bonding studies
R34E/ E36K/ R37E
mutations in linker region, mutant is inactive and insensitive to pH
S196C/G334C
site-directed mutagenesis, the Cys-engineered mutant is used for interdomain disulfide covalent bonding studies
Y29A
the point mutation is an activating mutation in full-length KinA, but interfers with KinA PAS-A dimerization shifting the PAS-A monomer/dimer equilibrium significantly toward the monomeric form
G192C/G334C
-
site-directed mutagenesis, the Cys-engineered mutant is used for interdomain disulfide covalent bonding studies
-
I108A
-
the point mutation does not affect KinA autophosphorylation activity, but interfers with KinA PAS-A dimerization
-
I95A
-
the point mutation slightly reduces the KinA autophosphorylation activity and interfers with KinA PAS-A dimerization
-
I95E
-
the point mutation reduces the KinA autophosphorylation activity and interfers with KinA PAS-A dimerization
-
K32E/E36K
-
mutations in linker region, mutant shows higher activity at higher pH and maintains pH regulation
-
Q193C/G334C
-
site-directed mutagenesis, the Cys-engineered mutant is used for interdomain disulfide covalent bonding studies
-
R34E/ E36K/ R37E
-
mutations in linker region, mutant is inactive and insensitive to pH
-
Y29A
-
the point mutation is an activating mutation in full-length KinA, but interfers with KinA PAS-A dimerization shifting the PAS-A monomer/dimer equilibrium significantly toward the monomeric form
-
H1172Q
mutation abolishes BvgS activity in vivo and eliminates detectable phosphorylation of BvgA in vitro. Activity of BvgS H1172Q can be restored by providing the wild-type C-terminal domain in trans
C69A
A287C/L333C
-
site-directed mutagenesis, the mutant cross-linked dimer shows altered autophosphorylation activity compared to the wild-type enzyme
I286C
-
site-directed mutagenesis of the long HK domain version, the mutation is located in the alpha1 helix N-terminal to the histidine phosphoacceptor, the mutant cross-linked dimer shows altered autophosphorylation activity compared to the wild-type enzyme
I286C/N388A
-
site-directed mutagenesis of the short HK domain version, the N388A mutation impairs the phosphorylation capacity, the mutant is unable to bind ATP
V282C
-
site-directed mutagenesis, the mutation is located in the alpha1 helix N-terminal to the histidine phosphoacceptor, the mutant cross-linked dimer shows altered autophosphorylation activity compared to the wild-type enzyme
D286C
-
t1/2 at room temperature is 16 min, compared to 12 min for wild-type enzyme. 71% of the wild-type phosphatase activity
E257C
-
t1/2 at room temperature is 30 min, compared to 12 min for wild-type enzyme. 31% of the wild-type phosphatase activity
E261C
-
t1/2 at room temperature is 15 min, compared to 12 min for wild-type enzyme. 77% of the wild-type phosphatase activity
E268C
-
t1/2 at room temperature is 23 min, compared to 12 min for wild-type enzyme. 45% of the wild-type phosphatase activity
E275C
-
t1/2 at room temperature is 28 min, compared to 12 min for wild-type enzyme. 34% of the wild-type phosphatase activity
E276C
-
t1/2 at room temperature is 68 min, compared to 12 min for wild-type enzyme. 5% of the wild-type phosphatase activity
E282C
-
t1/2 at room temperature is 15 min, compared to 12 min for wild-type enzyme. 77% of the wild-type phosphatase activity
F43I
site-directed mutagenesis, the mutation results in a slightly reduced growth defect compared to the construct in which all interface binding site residues are mutated
G240C
-
t1/2 at room temperature is 10 min, compared to 12 min for wild-type enzyme. 123% of the wild-type phosphatase activity
G264C
-
t1/2 at room temperature is 12 min, compared to 12 min for wild-type enzyme. As active as wild-type enzyme
H153F
mutation in periplasmic arm, mutant does not show any detectable activity above background at pH 7 or pH 5.6
H176A
site-directed mutagenesis, the mutation results in the same growth defects as the construct in which all interface binding site residues are mutated
H226Q/S600I
level of activity at pH 7 is very similar to that of EvgS S600I and mutant is inducible at pH 5.6
H243X
the His residue at position 243 of the EnvZ protein is changed by means of site-directed mutagenesis. The mutant EnvZ protein is defective in its in vitro ability not only as to EnvZ-autophosphorylation but also OmpR-phosphorylation and OmpR-dephosphorylation. This particular mutant EnvZ protein seems to exhibit null functions as to the in vivo osmoregulatory phenotype
H248A
-
mutation abrogates autophosphorylation by disrupting the phosphorylation site in the DHp domain
H398L
-
the mutant retains itscapability to bind ATP and is competent to catalyze the transphosphorylation of an AtoS G-box (G565A) mutant protein which otherwise fails to autophosphorylate due to its inability to bind ATP
H42A
site-directed mutagenesis, the mutation results in the same growth defects as the construct in which all interface binding site residues are mutated
H63Q/H106Q/H124Q
mutations in potential His triad, mutant shows the same level of induction as the wild-type EvgS
K152A
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows moderate activation by KCl-supplemented M9 medium, pH 5.5
K152E
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows strong activation by KCl-supplemented M9 medium, pH 5.5
K152F
naturally occuring mutation and site-directed mutagenesis, in the mutant, EvgS activation is observed only by complementation with pBADevgS, mutation L152F leads to the desensitization of EvgS in strain KMY1. The mutant shows no activation by KCl-supplemented M9 medium, pH 5.5. The L152F mutation is found in only two Escherichia coli strains, MC4100 and DH1
K152I
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows strong activation by KCl-supplemented M9 medium, pH 5.5
K152R
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows moderate activation by KCl-supplemented M9 medium, pH 5.5
K152Y
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows no activation by KCl-supplemented M9 medium, pH 5.5
K272C
-
t1/2 at room temperature is 55 min, compared to 12 min for wild-type enzyme. 10% of the wild-type phosphatase activity
L152F/S600I
level of activity at pH 7 is very similar to that of EvgS S600I and mutant is inducible at pH 5.6
L236C
-
t1/2 at room temperature is 25 min, compared to 12 min for wild-type enzyme. 40% of the wild-type phosphatase activity
L254C
-
inactive mutant enzyme, t1/2 at room temperature is 90 min, compared to 12 min for wild-type enzyme
N271C
-
t1/2 at room temperature is 36 min, compared to 12 min for wild-type enzyme. 23% of the wild-type phosphatase activity
N278C
-
t1/2 at room temperature is 45 min, compared to 12 min for wild-type enzyme. 15% of the wild-type phosphatase activity
N356K
-
mutation abrogates autophosphorylation by disrupting the ATP-binding site in the CA domain
P522A/S600I
level of activity at pH 7 is very similar to that of EvgS S600I and mutant is inducible at pH 5.6
Q262C
-
t1/2 at room temperature is 11 min, compared to 12 min for wild-type enzyme. 111% of the wild-type phosphatase activity
Q283C
-
t1/2 at room temperature is 13 min, compared to 12 min for wild-type enzyme. 91% of the wild-type phosphatase activity
R246C
-
t1/2 at room temperature is 62 min, compared to 12 min for wild-type enzyme. 7% of the wild-type phosphatase activity
S242C
-
t1/2 at room temperature is 39 min, compared to 12 min for wild-type enzyme. 20% of the wild-type phosphatase activity
S260C
-
t1/2 at room temperature is 13 min, compared to 12 min for wild-type enzyme. 91% of the wild-type phosphatase activity
S269C
-
t1/2 at room temperature is 20 min, compared to 12 min for wild-type enzyme. 54% of the wild-type phosphatase activity
S600I
mutation in cytoplasmic PAS domain, renders EvgS constitutively active at pH 7
T235C
-
t1/2 at room temperature is 14 min, compared to 12 min for wild-type enzyme. 84% of the wild-type phosphatase activity
T250C
-
t1/2 at room temperature is 23 min, compared to 12 min for wild-type enzyme. 45% of the wild-type phosphatase activity
T256C
-
t1/2 at room temperature is 27 min, compared to 12 min for wild-type enzyme. 36% of the wild-type phosphatase activity
Y265C
-
t1/2 at room temperature is 20 min, compared to 12 min for wild-type enzyme. 54% of the wild-type phosphatase activity
H44A
-
the mutation may increase the side chain pKa of acidic amino acids in the input domain, whose protonation contributes to the activation of ArsS
D56N
phosphorylation of CitB is inhibited by a D56N exchange. In the presence of ATP, CitB-D56N forms a stable complex with MalE-CitAC
H350L
autokinase activity of CitA is abolished by an H350L exchange
D657N
-
substitution in the first receiver domain, is unable to complement the deltarodK strain SA1708, delayed timing of aggregation, rare sporulation outside fruiting bodies, but normal fruiting body morphology on CF agar, loose aggregates of fruiting bodies in submerged culutre
D657N/D782N
-
delayed timing of aggregation, frequent sporulation outside fruiting bodies, and loose mounds of fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre, no autophosphorylation
D657N/D782N/D909N
-
delayed timing of aggregation, frequent sporulation outside fruiting bodies, and irregular fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre, autophosphorylates
D657N/D909N
-
delayed timing of aggregation, frequent sporulation outside fruiting bodies, and irregular and small fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre, autophosphorylates
D696A
site-directed mutagenesis, the mutation of the receiver domain residue leads to release of phosphate to the medium, overview
D782N
-
substitution in the second receiver domain, is unable to complement the deltarodK strain SA1708, delayed timing of aggregation, frequent sporulation outside fruiting bodies, and irregular and small fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre
D782N/D909N
-
delayed timing of aggregation, frequent sporulation outside fruiting bodies, and loose mounds of fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre, autophosphorylates
D909N
-
substitution in the third receiver domain, is unable to complement the deltarodK strain SA1708, delayed timing of aggregation, frequent sporulation outside fruiting bodies, but normal fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre
H360A
-
is unable to complement the deltarodK strain SA1708, delayed timing of aggregation, frequent sporulation outside fruiting bodies, and irregular fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre
H407A
site-directed mutagenesis, the mutation of the autophosphorylation site residue H407 inhibits autophosphorylation of the enzyme
A143G
-
the mutant still has some divalent cation-mediated repression and therefore likely has some ability to bind cations
D110A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
D131A
D60C
contrary to wild-type, mutant strain displays Co(II)-inducible resistance to antibiotic meropenem
E115A
-
the mutant still has some divalent cation-mediated repression and therefore likely has some ability to bind cations
E133A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
E77A
-
the mutant still has some divalent cation-mediated repression and therefore likely has some ability to bind cations
G139A
-
the mutant still has some divalent cation-mediated repression and therefore likely has some ability to bind cations
H124A
no change in overall periplasmic domain fold, mutant shows an altered biofilm morphology compared to the wild-type strain
H133A
no change in overall periplasmic domain fold, mutant abolishes biofilm formation
H55A
mutant loses its intrinsic resistance to Zn(II) and meropenem due to the destruction of Zn(II) binding site
L137A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
L158A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
L38C/H55A
mutation L38C restores the lost responsiveness of mutation H55A to Zn(II) stimulus
Q188L
site-directed mutagenesis, crystal structure determination and analysis
R94A
mutant strain shows biofilm morphology similar to wild-type
S145A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
D60C
-
contrary to wild-type, mutant strain displays Co(II)-inducible resistance to antibiotic meropenem
-
H124A
-
no change in overall periplasmic domain fold, mutant shows an altered biofilm morphology compared to the wild-type strain
-
H133A
-
no change in overall periplasmic domain fold, mutant abolishes biofilm formation
-
H55A
-
mutant loses its intrinsic resistance to Zn(II) and meropenem due to the destruction of Zn(II) binding site
-
L38C/H55A
-
mutation L38C restores the lost responsiveness of mutation H55A to Zn(II) stimulus
-
R94A
-
mutant strain shows biofilm morphology similar to wild-type
-
H146R/H147R/H149R
the mutant shows minimal copper inducibility compared to wild type CinS
H147R
the mutation has an almost 10fold reduced copper-dependent induction of cinAQ compared to the wild type
H147R/H149R
the mutant shows minimal copper inducibility compared to wild type CinS
H37R
the mutation has an almost 10fold reduced copper-dependent induction of cinAQ compared to the wild type
H146R/H147R/H149R
-
the mutant shows minimal copper inducibility compared to wild type CinS
-
H147R
-
the mutation has an almost 10fold reduced copper-dependent induction of cinAQ compared to the wild type
-
H147R/H149R
-
the mutant shows minimal copper inducibility compared to wild type CinS
-
H37R
-
the mutation has an almost 10fold reduced copper-dependent induction of cinAQ compared to the wild type
-
A143G
-
the mutant still has some divalent cation-mediated repression and therefore likely have some ability to bind cations
D110A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
D131A
E115A
-
the mutant still has some divalent cation-mediated repression and therefore likely have some ability to bind cations
E133A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
E77A
-
the mutant still has some divalent cation-mediated repression and therefore likely have some ability to bind cations
G139A
-
the mutant still has some divalent cation-mediated repression and therefore likely have some ability to bind cations
L137A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
L158A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
S145A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
H271Y
introducing the mutation into wild-type activates the WalKR regulon. Zn2+ is tetrahedrally-coordinated by four amino acids including H271. The H271Y mutation abrogates metal binding, increasing WalK kinase activity and WalR phosphorylation. The mutant strain shows increased lysostaphin and vancomycin sensitivity
N44C/G142C
site-directed mutagenesis, the monomeric band intensities of the double mutant are dramatically decreased
N44C/G143C
site-directed mutagenesis, the monomeric band intensities of the double mutant are dramatically decreased
N44C/R146C
site-directed mutagenesis, introducing cysteine substitution at Arg146 of YycG N44C mutant does not show any high molecular weight bands, but it shows only the dimeric band of YycG N44C
N44C/G142C
-
site-directed mutagenesis, the monomeric band intensities of the double mutant are dramatically decreased
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N44C/G143C
-
site-directed mutagenesis, the monomeric band intensities of the double mutant are dramatically decreased
-
N44C/R146C
-
site-directed mutagenesis, introducing cysteine substitution at Arg146 of YycG N44C mutant does not show any high molecular weight bands, but it shows only the dimeric band of YycG N44C
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D326A/N337A
site-directed mutagenesis, the mutant is inactive in autophosphorylation
D326A/Q330A
site-directed mutagenesis, the mutant shows highly reduced autophosphorylation activity compared to the wild-type enzyme
F383A/R385A
site-directed mutagenesis, the mutant shows highly reduced autophosphorylation activity compared to the wild-type enzyme
N334A/N337A
site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation
P222A
site-directed mutagenesis, the mutation eliminates the phosphatase activity of the enzyme
P222G
site-directed mutagenesis, the mutant shows phosphatase activity similar to the wild-type enzyme
Q297A/I298A
site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation
R294A
site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation
R382A/R385A
T221A
site-directed mutagenesis, the mutation eliminates the phosphatase activity but does not affect the autokinase activity of the enzyme
D326A/Q330A
-
site-directed mutagenesis, the mutant shows highly reduced autophosphorylation activity compared to the wild-type enzyme
-
N334A/N337A
-
site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation
-
Q297A/I298A
-
site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation
-
R294A
-
site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation
-
R382A/R385A
-
site-directed mutagenesis, the mutant shows highly reduced autophosphorylation activity compared to the wild-type enzyme
-
D326A/N337A
site-directed mutagenesis, the mutation abolishes VicK autokinase activity
D326A/Q330A
site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity
F383A/R385A
site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity
I403S
site-directed mutagenesis, the mutation does not significantly affect VicK autokinase activity
I403W
site-directed mutagenesis, the mutation does not significantly affect VicK autokinase activity but dramatically increases autokinase activity in HK853
K341A/Y342A
site-directed mutagenesis, the mutation negatively affects autokinase activity
N334A/N337A
site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type
P222A
site-directed mutagenesis, the mutant abolishes enzyme VicK's phosphatase activity
P222G
site-directed mutagenesis, the mutant retains full autokinase activity when compared to wild-type, but the mutation abolishes the VicK phosphatase activity
Q297A/I298A
site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type
R294A
site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type
R382A/R385A
T221A
site-directed mutagenesis, the mutant retains full autokinase activity but the enzyme VicK's phosphatase activity is abolished
T221A/P222A/P222G/V212A/V215A/S213A/S216A
site-directed mutagenesis, the mutation only slightly reduces autokinase activity, while it abolishes the VicK phosphatase activity
V212A/V215A/S213A/S216A
site-directed mutagenesis, the mutation only slightly reduces autokinase activity, while it abolishes the VicK phosphatase activity
D326A/N337A
-
site-directed mutagenesis, the mutation abolishes VicK autokinase activity
-
D326A/Q330A
-
site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity
-
F383A/R385A
-
site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity
-
R382A/R385A
E105A
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E105L
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E105Q
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E107A
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E107L
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E107Q
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E83A
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E83L
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E83L/E105L/E107A
site-directed mutagenesis, the mutant is pH-independent and mimics the low pH structure
E83Q
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E105A
-
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
-
E83A
-
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
-
E83L
-
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
-
E83L/E105L/E107A
-
site-directed mutagenesis, the mutant is pH-independent and mimics the low pH structure
-
E83Q
-
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
-
D156A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
D300A
site-directed mutagenesis, the mutation might change the dimeric configuration of the PAS domain, thereby enhancing the negative effect on kinase activity. The D300A-mutated PAS domain of Hik33 also forms dimer in the assay. The Hik33n-SphSc mutant shows reduced expression under non-stressed and salt-stressed conditions compared to unaltered Hik33n-SphSc
D389A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
D412N
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
E416Q
site-directed mutagenesis, the Hik33n-SphSc mutant shows normal expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
G123A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
G405A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
G405S
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and no expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
N309A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
P114A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
Q141A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
Q22A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2nHik7c construct is inactive in alkaline phosphatase activity
Q411E
site-directed mutagenesis, the Hik33n-SphSc mutant shows normal expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
R129K
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
R377A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
R400S/R404A
site-directed mutagenesis, the Hik33n-SphSc mutant shows normal expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
R404A
site-directed mutagenesis, the Hik33n-SphSc mutant shows normal expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
R415E
site-directed mutagenesis, the mutation might change the dimeric configuration of the PAS domain, thereby enhancing the negative effect on kinase activity. The Hik33n-SphSc mutant shows reduced expression under non-stressed and salt-stressed conditions compared to unaltered Hik33n-SphSc
T409V
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and no expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
T414V
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and no expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
V395A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
W134F
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
W318A
site-directed mutagenesis, the mutation might change the dimeric configuration of the PAS domain, thereby enhancing the negative effect on kinase activity. The W318A-mutated PAS domain of Hik33 also forms dimer in the assay. The Hik33n-SphSc mutant shows reduced expression under non-stressed and salt-stressed conditions compared to unaltered Hik33n-SphSc
D449A
-
site-directed mutagenesis, the mutation in the ATP-binding pocket prevents nucleotide binding
H405Y
-
site-directed mutagenesis, the mutation abrogates the kinase activity
H45K
-
site-directed mutagenesis, a CheAFL variant that lacks the substrate His
H45K/H405Y
-
site-directed mutagenesis, the mutant shows reduced kinase activity compared to the wild-type
additional information
S147L
a BA2291 mutant, which mimics the behavior of the overexpressed wild-type protein.The S147L mutation does not affect the interaction of the kinase with Spo0F or the rate of phosphoryl group transfer to it
S147L
-
a BA2291 mutant, which mimics the behavior of the overexpressed wild-type protein.The S147L mutation does not affect the interaction of the kinase with Spo0F or the rate of phosphoryl group transfer to it
-
H188V
the mutant retains the phosphatase activity of the wild type protein, the mutation triggers formation of an N-terminal 2-helical coiled-coil and extensive dimerization and histidine phosphotransfer domain-ATP-binding domain association
C69A
-
mutant in LOV-HK knockout background does not return the replication rate to the wild-type level
C69A
-
LOV-HK mutant, binds flavin mononucleotide but cannot form the cysteinyl adduct, does not activate the kinase in response to illumination
D131A
-
the purified mutant enzyme shows no fluorescence change well into the mM range of Mg2+, suggesting that this mutation renders the protein incapable of binding Mg2+
D131A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
D131A
-
the purified mutant enzyme shows no fluorescence change well into the mM range of Mg2+, suggesting that this mutation renders the protein incapable of binding Mg2+
D131A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
R382A/R385A
site-directed mutagenesis, the mutant shows highly reduced autophosphorylation activity compared to the wild-type enzyme
R382A/R385A
site-directed mutagenesis, the mutant is inactive in autophosphorylation
R382A/R385A
site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity
R382A/R385A
site-directed mutagenesis, the mutation abolishes VicK autokinase activity
R382A/R385A
-
site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity
-
R382A/R385A
-
site-directed mutagenesis, the mutation abolishes VicK autokinase activity
-
additional information
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removal of the first 280 amino acids of VirA, referred to as VirA(LKR), and further removal of the charged residues VirA(LKR)D280-284, preserves basic wild-type induction in response to acetosyringone. Further truncation to VirA(LKR)D280-293 eliminates induction by acetosyringone while increasing the induction of 2,6-dimethoxyphenol, which lacks the para substituent of acetosyringone. Construction of the truncated construct VirA(LKR)D280-284, amino acid residues 285-293 are randomly mutagenized, and the resulting colonies are probed for altered specificity in a sequential phenol specificity screen
additional information
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removal of the first 280 amino acids of VirA, referred to as VirA(LKR), and further removal of the charged residues VirA(LKR)D280-284, preserves basic wild-type induction in response to acetosyringone. Further truncation to VirA(LKR)D280-293 eliminates induction by acetosyringone while increasing the induction of 2,6-dimethoxyphenol, which lacks the para substituent of acetosyringone. Construction of the truncated construct VirA(LKR)D280-284, amino acid residues 285-293 are randomly mutagenized, and the resulting colonies are probed for altered specificity in a sequential phenol specificity screen
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additional information
construction of enzyme-deficient mutant strain rscS*DELTAbinK sypG::Tnerm, competition assays of wild-type and mutant strains in vitro and in vivo, overview. DELTAbinK has no effect in the pSypG sypE+ background
additional information
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construction of enzyme-deficient mutant strain rscS*DELTAbinK sypG::Tnerm, competition assays of wild-type and mutant strains in vitro and in vivo, overview. DELTAbinK has no effect in the pSypG sypE+ background
additional information
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construction of enzyme-deficient mutant strain rscS*DELTAbinK sypG::Tnerm, competition assays of wild-type and mutant strains in vitro and in vivo, overview. DELTAbinK has no effect in the pSypG sypE+ background
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additional information
generation of an enzyme deletion mutant strain by gene disruption of AaHSK1 using a hygromycin phosphotransferase gene (HYG) cassette
additional information
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generation of an enzyme deletion mutant strain by gene disruption of AaHSK1 using a hygromycin phosphotransferase gene (HYG) cassette
additional information
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generation of an enzyme deletion mutant strain by gene disruption of AaHSK1 using a hygromycin phosphotransferase gene (HYG) cassette
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additional information
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construction of ahk5 T-DNA insertion mutants, Arabidopsis mutants lacking AHK5 show reduced stomatal closure in response to H2O2, which is reversed by complementation with the wild type gene. Overexpression of AHK5 results in constitutively less stomatal closure. Abiotic stimuli that generate endogenous H2O2, such as darkness, nitric oxide and the phytohormone ethylene, also show reduced stomatal closure in the ahk5 mutants. However, ABA causes closure, dark adaptation induces H2O2 production and H2O2 induces NO synthesis in mutants, phenotype, overview
additional information
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generation of CKI1 loss-of-function mutants. Transformation of egg cell to central cell by ectopic CKI1 retains female gametophyte organization
additional information
generation of the ahk5-1 mutant containing a T-DNA insertion in the receiver domain of the AHK5 histidine kinase. The AHK5 mutant is more resistant to salt stress. Two complemented lines, PAHK5-AHK5/ahk5-1-1 and PAHK5-AHK5/ahk5-1-4, are generated by complementation of the ahk5-1 mutant with full-length AHK5 including 3205 bases upstream of the ATG start codon
additional information
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generation of the ahk5-1 mutant containing a T-DNA insertion in the receiver domain of the AHK5 histidine kinase. The AHK5 mutant is more resistant to salt stress. Two complemented lines, PAHK5-AHK5/ahk5-1-1 and PAHK5-AHK5/ahk5-1-4, are generated by complementation of the ahk5-1 mutant with full-length AHK5 including 3205 bases upstream of the ATG start codon
additional information
the T-DNA insertion is transmitted through female gametophytes at an extremely low frequency in CKI1/cki1-8 plants, while cki1-6 mutation, which carries a T-DNA at a more distal location in the CKI1 promoter than cki1-8 mutatin does not appear to be capable of being transmitted through female gametophytes. The cki1-8 mutation impairs female gametophyte development, cki1-8 mutant phenotype during reproductive development and vegetative growth. Mutant phenotypes, overview
additional information
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generation of the ahk5-1 mutant containing a T-DNA insertion in the receiver domain of the AHK5 histidine kinase. The AHK5 mutant is more resistant to salt stress. Two complemented lines, PAHK5-AHK5/ahk5-1-1 and PAHK5-AHK5/ahk5-1-4, are generated by complementation of the ahk5-1 mutant with full-length AHK5 including 3205 bases upstream of the ATG start codon
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additional information
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the T-DNA insertion is transmitted through female gametophytes at an extremely low frequency in CKI1/cki1-8 plants, while cki1-6 mutation, which carries a T-DNA at a more distal location in the CKI1 promoter than cki1-8 mutatin does not appear to be capable of being transmitted through female gametophytes. The cki1-8 mutation impairs female gametophyte development, cki1-8 mutant phenotype during reproductive development and vegetative growth. Mutant phenotypes, overview
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additional information
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generation of CKI1 loss-of-function mutants. Transformation of egg cell to central cell by ectopic CKI1 retains female gametophyte organization
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additional information
the BA2291 gene is capable of complementing Bacillus subtilis sporulation kinase-deficient mutants when present in the cell in single copy, and its deletion in Bacillus anthracis strongly reduces the ability of the organism to sporulate. BA2291 overexpression in Bacillus subtilis completely prevents sporulation, also in a wild type strain
additional information
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the BA2291 gene is capable of complementing Bacillus subtilis sporulation kinase-deficient mutants when present in the cell in single copy, and its deletion in Bacillus anthracis strongly reduces the ability of the organism to sporulate. BA2291 overexpression in Bacillus subtilis completely prevents sporulation, also in a wild type strain
additional information
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the BA2291 gene is capable of complementing Bacillus subtilis sporulation kinase-deficient mutants when present in the cell in single copy, and its deletion in Bacillus anthracis strongly reduces the ability of the organism to sporulate. BA2291 overexpression in Bacillus subtilis completely prevents sporulation, also in a wild type strain
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additional information
YycG depletion does not interfere with FtsZ localization, YycG is less active as a kinase of YycF in the absence of a division septum
additional information
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YycG depletion does not interfere with FtsZ localization, YycG is less active as a kinase of YycF in the absence of a division septum
additional information
a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking the N-terminal Per-ARNT-Sim domain, which plays a critical role in the catalytic activity of this enzyme
additional information
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a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking the N-terminal Per-ARNT-Sim domain, which plays a critical role in the catalytic activity of this enzyme
additional information
deletion in the abrB gene suppresses the DELTAkinD mutation
additional information
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deletion in the abrB gene suppresses the DELTAkinD mutation
additional information
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in vivo quantitative domain-based stepwise deletion analyses to determine the minimum functional domain of KinC, overview
additional information
generation of a KinD-DegS hybrid kinase using overlapping PCR, overview. DegS is a sensory histidine kinase that is able to phosphorylate DegU, a DNA-binding response regulator. The DegS-DegU system controls many genes (both positively and negatively) including the fla/che operon that encodes dozens of genes involved in motility and chemotaxis
additional information
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generation of a KinD-DegS hybrid kinase using overlapping PCR, overview. DegS is a sensory histidine kinase that is able to phosphorylate DegU, a DNA-binding response regulator. The DegS-DegU system controls many genes (both positively and negatively) including the fla/che operon that encodes dozens of genes involved in motility and chemotaxis
additional information
generation of several truncation mutant of enzyme YycG. All truncated YycG constructs including the shortest one that featured only the cytoplasmic PAS and the two catalytic HisKA and HATPase domains retain the ability to localize to the septum. N-terminal truncations of YycG lose negative regulation of their activity, truncated YycG constructs fail to co-immunoprecipitate with the regulatory proteins YycH and YycI
additional information
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generation of several truncation mutant of enzyme YycG. All truncated YycG constructs including the shortest one that featured only the cytoplasmic PAS and the two catalytic HisKA and HATPase domains retain the ability to localize to the septum. N-terminal truncations of YycG lose negative regulation of their activity, truncated YycG constructs fail to co-immunoprecipitate with the regulatory proteins YycH and YycI
additional information
a truncated version of DesK, which lacks the transmembrane domain, is not pH-dependent
additional information
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a truncated version of DesK, which lacks the transmembrane domain, is not pH-dependent
additional information
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a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking the N-terminal Per-ARNT-Sim domain, which plays a critical role in the catalytic activity of this enzyme
-
additional information
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deletion in the abrB gene suppresses the DELTAkinD mutation
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additional information
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generation of a KinD-DegS hybrid kinase using overlapping PCR, overview. DegS is a sensory histidine kinase that is able to phosphorylate DegU, a DNA-binding response regulator. The DegS-DegU system controls many genes (both positively and negatively) including the fla/che operon that encodes dozens of genes involved in motility and chemotaxis
-
additional information
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generation of several truncation mutant of enzyme YycG. All truncated YycG constructs including the shortest one that featured only the cytoplasmic PAS and the two catalytic HisKA and HATPase domains retain the ability to localize to the septum. N-terminal truncations of YycG lose negative regulation of their activity, truncated YycG constructs fail to co-immunoprecipitate with the regulatory proteins YycH and YycI
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additional information
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in vivo quantitative domain-based stepwise deletion analyses to determine the minimum functional domain of KinC, overview
-
additional information
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a truncated version of DesK, which lacks the transmembrane domain, is not pH-dependent
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additional information
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bos1-null mutants, osmosensitivity and resistance to fungicides, very rarely form conidiophores and those few conidiophores fail to produce conidia, this defect can be partially restored with 1000 mM sorbitol. Mutants are not hypersensitive to various oxidative stresses but are more resistant to menadione, have significantly reduced ability to infect host plants. Appressorium morphogenesis is not altered, however, in planta growth is severely reduced
additional information
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bos1-null mutants, osmosensitivity and resistance to fungicides, very rarely form conidiophores and those few conidiophores fail to produce conidia, this defect can be partially restored with 1000 mM sorbitol. Mutants are not hypersensitive to various oxidative stresses but are more resistant to menadione, have significantly reduced ability to infect host plants. Appressorium morphogenesis is not altered, however, in planta growth is severely reduced
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additional information
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deletion of the pdhS in the presence of a rescue copy expressed from pRH232, pRH232 is replaced in the deltapdhS strain only in the presence of another wild-type copy of pdhS through pRH404
additional information
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insertion-knockout mutant strain by introduction of a kanamycin-resistant cassette into the gene, replication is less than the wild-type strain as early as 4 hours after infection with J774A.1 murine macrophages
additional information
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deletion of the pdhS in the presence of a rescue copy expressed from pRH232, pRH232 is replaced in the deltapdhS strain only in the presence of another wild-type copy of pdhS through pRH404
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additional information
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generation of two different versions of the HK domain: one long (L, the HK domain plus a 23-kDa tag, 49 kDa) and other short (S, 26 kDa). The short version has the N388A mutation which impairs the phosphorylation capacity. Both versions have the I286C mutation
additional information
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the disruption of a PAS-like motif in the sensor domain affects the stability of CckA accumulation at the poles accompanied by a partial loss in CckA function. Shortening of an extended linker between beta-sheets within the CckA catalysis-assisting ATP-binding domain leads to a dramatic cell-to-cell variability in CpdR levels and CtrA cell cycle periodicity
additional information
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in the deltamtrAB mutant, the expression of carrier genes is abolished (betP) or markedly reduced, MtrB mutants in which either the large periplasmic loop or the HAMP domain is deleted, are regulated similar to wild-type MtrB
additional information
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ethanolamine utilization and growth on it is abolished in the response regulator RR17 mutant strain lacking a functional partner of histidine kinase in the RR-HK17 two-component system, phenotype, overview
additional information
cheA mutations leading to defects in chemotaxis are mapped and characterized
additional information
the histidine phosphorylation sites of each TorS transmitter domain and the aspartate phosphorylation site of the TorS receiver are individually changed by site-directed mutagenesis. All three phosphorylation sites proved essential for in vivo induction of the tor structural operon and for in vitro transphosphorylation of the cognate TorR response regulator. The His to Gln change in the classical transmitter domain abolished TorS autophosphorylation, whereas TorS undergoes significant autophosphorylation when the phosphorylation site of its receiver or alternative transmitter is changed
additional information
construction of several phoR genes, with various deletions in the 5' regions, which are regulated by the trp-lac hybrid promoter. The PhoR1084 and PhoR1159 proteins that lack the 83 and 158 N-terminal amino acids, respectively, retain the positive function for the expression of phoA that codes for alkaline phosphatase, but lack the negative function. The PhoR1263 protein that lacks the 262 N-terminal amino acids is deficient in both functions
additional information
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mutations within the linker HAMP domain block the osmosensing function of EnvZ
additional information
construction of a DELTAcusS enzyme nockout mutant in an Escherichia coli strain in which the chromosomal copy of the gene for the multicopper oxidase CueO has been deleted (DELTAcueO). CueO converts Cu(I) to Cu(II) and therefore the use of the strain with the cueO deletion allows the observation of a growth phenotype even under aerobic conditions. The chromosomal copy of cusS is deleted from this background strain to allow characterization of CusS variants expressed from a plasmid. Partial functional complementation ofthe mutant strain with lasmid-expressed wild-type enzyme. The mutations do not significantly affect the relative expression levels of CusS
additional information
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construction of a DELTAcusS enzyme nockout mutant in an Escherichia coli strain in which the chromosomal copy of the gene for the multicopper oxidase CueO has been deleted (DELTAcueO). CueO converts Cu(I) to Cu(II) and therefore the use of the strain with the cueO deletion allows the observation of a growth phenotype even under aerobic conditions. The chromosomal copy of cusS is deleted from this background strain to allow characterization of CusS variants expressed from a plasmid. Partial functional complementation ofthe mutant strain with lasmid-expressed wild-type enzyme. The mutations do not significantly affect the relative expression levels of CusS
additional information
construction of EvgS-PhoQ chimeras and activation of these chimera sensors, overview. The EvgS sensor domain is fused to the cytoplasmic region of PhoQ to examine whether it still responded to the signals. In chimera PvgS-A, the region from the N terminus to the transmembrane region of EvgS (residues 1 to 558 of EvgS) is fused to the cytoplasmic region of PhoQ (residues 215 to 486 of PhoQ) comprising the HAMP, HisKA, and HATPase_c domains, and in chimera PvgS-B, the region from the N terminus to the linker domain of EvgS (residues 1 to 710 of EvgS) is fused to the HisKA and HATPase_c domains of PhoQ (residues 267 to 486 of PhoQ)
additional information
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construction of EvgS-PhoQ chimeras and activation of these chimera sensors, overview. The EvgS sensor domain is fused to the cytoplasmic region of PhoQ to examine whether it still responded to the signals. In chimera PvgS-A, the region from the N terminus to the transmembrane region of EvgS (residues 1 to 558 of EvgS) is fused to the cytoplasmic region of PhoQ (residues 215 to 486 of PhoQ) comprising the HAMP, HisKA, and HATPase_c domains, and in chimera PvgS-B, the region from the N terminus to the linker domain of EvgS (residues 1 to 710 of EvgS) is fused to the HisKA and HATPase_c domains of PhoQ (residues 267 to 486 of PhoQ)
additional information
construction of a functional chimeric protein, equivalent to the full cytosolic part of EnvZ, encompassing the entire catalytic part of the Escherichia coli EnvZ histidine kinase, fused to the HAMP domain of the Archaeoglobus fulgidus Af1503 receptor, generation of a second chimeric mutant version with additional A291F exchange
additional information
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construction of a functional chimeric protein, equivalent to the full cytosolic part of EnvZ, encompassing the entire catalytic part of the Escherichia coli EnvZ histidine kinase, fused to the HAMP domain of the Archaeoglobus fulgidus Af1503 receptor, generation of a second chimeric mutant version with additional A291F exchange
additional information
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engineering of covalent dimers of the cytoplasmic domains of CpxA which provide a robust experimental system for investigating cooperativity in histidine kinase autophosphorylation
additional information
His226 is required for induction and is structurally colocated with Pro522 at the top of the predicted transmembrane helix. The constitutive mutations in the PAS domain can be further activated by low external pH. Expression of the cytoplasmic part of the protein alone also gives constitutive activation, which is lost if the constitutive PAS mutations are present. The cytoplasmic part shows pH-dependent dimer formation in vitro
additional information
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His226 is required for induction and is structurally colocated with Pro522 at the top of the predicted transmembrane helix. The constitutive mutations in the PAS domain can be further activated by low external pH. Expression of the cytoplasmic part of the protein alone also gives constitutive activation, which is lost if the constitutive PAS mutations are present. The cytoplasmic part shows pH-dependent dimer formation in vitro
additional information
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growth of HP0244 mutant strain is similar to the growth of the wild-type strain, null mutations in either HP0165 or HP1364 histidine kinases are impaired in their ability to grow at pH 5.0, acid-responsive gene transcription is altered in the HP0165 and HP1364 null mutant strains compared to the parental wild-type strain, growth of complemented mutant strains is similar to that of the wild-type strain
additional information
an acid survival study using an HP0703 mutant and an electrophoretic mobility shift assay with in vitro-phosphorylated HP0703 showe, that HP0703 does not contribute to acid survival and does not bind to the promoter regions of several genes in the HP0244 pH-dependent regulon, suggesting that there is a pathway outside the HP0703 regulon which transduces the acid-responsive signal sensed by HP0244
additional information
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an acid survival study using an HP0703 mutant and an electrophoretic mobility shift assay with in vitro-phosphorylated HP0703 showe, that HP0703 does not contribute to acid survival and does not bind to the promoter regions of several genes in the HP0244 pH-dependent regulon, suggesting that there is a pathway outside the HP0703 regulon which transduces the acid-responsive signal sensed by HP0244
additional information
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delayed timing of aggregation, frequent sporulation outside fruiting bodies, and irregular fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre
additional information
construction of several mutants by in-frame deletions, espA mutants, encoding an orphan hybrid histidine kinase, alter the timing of the organism's developmental program, greatly accelerating developmental progression, phenotype, overview
additional information
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construction of several mutants by in-frame deletions, espA mutants, encoding an orphan hybrid histidine kinase, alter the timing of the organism's developmental program, greatly accelerating developmental progression, phenotype, overview
additional information
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deletion of 7 N-terminal enzyme residues affects dimer organization
additional information
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enzyme FimS from W83 is malfunctional and has a defective kinase domain due to a truncated conserved G3 box motif that provides an ATP-binding pocket. The introduction of the functional fimS from strain ATCC 33277 restores the production, but not polymerization, of endogenous FimA subunits in W83. Substantial expression of strain ATCC 33277-type FimA fimbriae in the strain W83 derivative requires the introduction and expression of the functional strain ATCC 33277 fimS
additional information
enzyme FimS from W83 is malfunctional and has a defective kinase domain due to a truncated conserved G3 box motif that provides an ATP-binding pocket. The introduction of the functional fimS from strain ATCC 33277 restores the production, but not polymerization, of endogenous FimA subunits in W83. Substantial expression of strain ATCC 33277-type FimA fimbriae in the strain W83 derivative requires the introduction and expression of the functional strain ATCC 33277 fimS
additional information
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enzyme FimS from W83 is malfunctional and has a defective kinase domain due to a truncated conserved G3 box motif that provides an ATP-binding pocket. The introduction of the functional fimS from strain ATCC 33277 restores the production, but not polymerization, of endogenous FimA subunits in W83. Substantial expression of strain ATCC 33277-type FimA fimbriae in the strain W83 derivative requires the introduction and expression of the functional strain ATCC 33277 fimS
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additional information
construction of diverse point, truncation, and deletion mutants of enzyme LadS, and generation of diverse two-hybrid constructs of enzyme LadS domains
additional information
construction of diverse point, truncation, and deletion mutants of enzyme LadS, and generation of diverse two-hybrid constructs of enzyme LadS domains
additional information
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construction of diverse point, truncation, and deletion mutants of enzyme LadS, and generation of diverse two-hybrid constructs of enzyme LadS domains
additional information
construction of diverse point, truncation, and deletion mutants of enzyme GacS, and generation of diverse two-hybrid constructs of enzyme GacS domains
additional information
construction of diverse point, truncation, and deletion mutants of enzyme GacS, and generation of diverse two-hybrid constructs of enzyme GacS domains
additional information
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construction of diverse point, truncation, and deletion mutants of enzyme GacS, and generation of diverse two-hybrid constructs of enzyme GacS domains
additional information
generation of a Shk1 deletion mutant, all the defects are restored by genetic complementation of the Shk1 deletion mutant with the wild-type Shk1 gene
additional information
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generation of a Shk1 deletion mutant, all the defects are restored by genetic complementation of the Shk1 deletion mutant with the wild-type Shk1 gene
additional information
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generation of a Shk1 deletion mutant, all the defects are restored by genetic complementation of the Shk1 deletion mutant with the wild-type Shk1 gene
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additional information
a point mutation in SaeS of strain Newman is responsible for increased expression of Eap upon exposure to sublethal Perform and SDS concentrations, leading to increased extracellular adherence protein-dependent cellular invasiveness
additional information
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a point mutation in SaeS of strain Newman is responsible for increased expression of Eap upon exposure to sublethal Perform and SDS concentrations, leading to increased extracellular adherence protein-dependent cellular invasiveness
additional information
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cross-linking of the recombinant the SeMet-substituted YycG enzyme
additional information
cross-linking of the recombinant the SeMet-substituted YycG enzyme
additional information
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construction of a truncated AgrCTM5-6C enzyme version, a hydrophobic polypeptide of 297 amino acids, that has two transmembrane helices connected by a small polar loop that is exposed to the periplasm
additional information
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a point mutation in SaeS of strain Newman is responsible for increased expression of Eap upon exposure to sublethal Perform and SDS concentrations, leading to increased extracellular adherence protein-dependent cellular invasiveness
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additional information
deletion of the first G loop (del392-395, RAQG) negatively affects autokinase activity
additional information
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genetic inactivation of covS decreases but does not eliminate CovR phosphorylation
additional information
generation of and draK gene deletion mutants, the gene disruption plasmids pKC-3063A and pKC-3062B are delivered into Streptomyces coelicolor A3(2) cells by conjugation with Escherichia coli ET12567(pUZ8002), and intergeneric conjugation between Escherichia coli and Streptomyces is performed, altered pH profile after acidic pH shock cultivation of the draR and draK gene deletion mutants, overview
additional information
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generation of and draK gene deletion mutants, the gene disruption plasmids pKC-3063A and pKC-3062B are delivered into Streptomyces coelicolor A3(2) cells by conjugation with Escherichia coli ET12567(pUZ8002), and intergeneric conjugation between Escherichia coli and Streptomyces is performed, altered pH profile after acidic pH shock cultivation of the draR and draK gene deletion mutants, overview
additional information
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construction of a senS disruption and a truncated mutant
additional information
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construction of a senS disruption and a truncated mutant
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additional information
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mutation of hik41 does not affect the expression of the genes located downstream of this gene, 22 H2O2-inducible genes are either totally or almost totally unresponsive to H2O2 in deltaHik33 mutant cells, whereas mutation of Hik34, Hik16 or Hik41 abolishes the H2O2 induction of only two genes, Hik16 and Hik41 regulate the H2O2-inducible expression of the same two genes
additional information
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inactivation of each putative hik gene, no significant alterations in gene expression in most of the mutants. DeltaHik33 and deltaHik19 exhibit reduced ability to activate luciferase at low temperature. Deltahik27, deltahik34, and deltahik20 show enhanced expression of some genes, whereas others are repressed. In deltaHik34 cells, levels of transcripts of heat-shock genes are elevated. In deltaHik33-, deltaHik34-, deltaHik16-, and deltaHik41-mutant cells gene expression is significantly affected by elevated levels of NaCl
additional information
construction of a fused sensor, Hik2n-Hik7c, which has the signal input domain of Hik2 and the kinase domain of the phosphate-deficiency sensor Hik7. The coding region of the hik7 gene is replaced with the fused sensor to evaluate the signalling activity in vivo as the activity of alkaline phosphatase (AP), which is regulated by Hik7. Cells expressing Hik2n-Hik7c have weak AP activities under standard growth conditions. Saline stress by NaCl induces AP activity in a dose-dependent manner. Hik2n-Hik7c responds to Cl- concentration. Amino acid substitutions in the signal input domain of Hik2 all result in loss of this responsiveness, i.e. mutants Q22A, P114A, G123A, R129K, W134F, Q141A and D156A completely lose AP activity
additional information
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construction of a fused sensor, Hik2n-Hik7c, which has the signal input domain of Hik2 and the kinase domain of the phosphate-deficiency sensor Hik7. The coding region of the hik7 gene is replaced with the fused sensor to evaluate the signalling activity in vivo as the activity of alkaline phosphatase (AP), which is regulated by Hik7. Cells expressing Hik2n-Hik7c have weak AP activities under standard growth conditions. Saline stress by NaCl induces AP activity in a dose-dependent manner. Hik2n-Hik7c responds to Cl- concentration. Amino acid substitutions in the signal input domain of Hik2 all result in loss of this responsiveness, i.e. mutants Q22A, P114A, G123A, R129K, W134F, Q141A and D156A completely lose AP activity
additional information
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generation of a series of chimeric proteins that include the N-terminal region of Hik33 (M1-A422) and the C-terminal region (Q197-P430) of SphS, a histidine kinase that senses phosphate-deficient conditions. The chimeric protein Hik33n-SphSc regulates expression of the phoA gene under stress conditions. Under standard growth conditions, cells that harbor the gene for Hik33n-SphSc express phoA, whereas the expression of phoA is repressed under salt stress and under cold stress
additional information
generation of a series of chimeric proteins that include the N-terminal region of Hik33 (M1-A422) and the C-terminal region (Q197-P430) of SphS, a histidine kinase that senses phosphate-deficient conditions. The chimeric protein Hik33n-SphSc regulates expression of the phoA gene under stress conditions. Under standard growth conditions, cells that harbor the gene for Hik33n-SphSc express phoA, whereas the expression of phoA is repressed under salt stress and under cold stress
additional information
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generation of a series of chimeric proteins that include the N-terminal region of stress regulator histidine kinase Hik33 (M1-A422) and the C-terminal region (Q197-P430) of SphS. The chimeric protein Hik33n-SphSc regulates expression of the phoA gene under stress conditions. Under standard growth conditions, cells that harbor the gene for Hik33n-SphSc express phoA, whereas the expression of phoA is repressed under salt stress and under cold stress
additional information
generation of a series of chimeric proteins that include the N-terminal region of stress regulator histidine kinase Hik33 (M1-A422) and the C-terminal region (Q197-P430) of SphS. The chimeric protein Hik33n-SphSc regulates expression of the phoA gene under stress conditions. Under standard growth conditions, cells that harbor the gene for Hik33n-SphSc express phoA, whereas the expression of phoA is repressed under salt stress and under cold stress
additional information
delta408ThkA, includes the PAS-sensor, the DHp and CA domains, and delta 517ThkA without the PAS-sensor domain, both are fully active in the autophosphorylation reaction
additional information
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delta408ThkA, includes the PAS-sensor, the DHp and CA domains, and delta 517ThkA without the PAS-sensor domain, both are fully active in the autophosphorylation reaction
additional information
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disulfide cross-linking of mutant enzymes, overview
additional information
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truncated His-RaxH, lacking the N-terminal transmembrane region, shows similar autophosphorylation activities than His-tagged full-length RaxH, but is unable to induce phosphorylation of His-RaxR
additional information
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truncated His-RaxH, lacking the N-terminal transmembrane region, shows similar autophosphorylation activities than His-tagged full-length RaxH, but is unable to induce phosphorylation of His-RaxR
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
HK2 is stable up to 40°C and reaches an intermediate state at 60°C. On raising the temperature to 100°C, the second stage of denaturation is observed
60
-
HK1 relatively stable up to 60°C, gets completely denatured at 90°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris-HCl buffer, pH 7.650 mM KCl, 10 mM MgCl2, 0.1 mM DTT, 2530% glycerol
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-80°C, 50 mM Tris/HCl buffer, pH 8.0, 500 mM NaCl, 10% glycerol, 10 mM beta-mercaptoethanol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by gel filtration
DEAE-agarose column chromatography, Ni-NTA column chromatography, glutathione-agarose resin column chromatography, and Superdex 200 gel filtration
-
full-length protein affinity-purified
glutathione Sepharose column chromatography and Superdex 75 gel filtration
HiTrap Ni2+-chelating column chromatography, Mono Q column chromatography, and Superdex 75 gel filtration
HiTrap Zn2+-chelating column chromatography, Superdex 75 gel filtration
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Ni-chelating Sepharose column chromatography and Sephacryl S300 gel filtration
-
Ni-NTA column chromatography and glutathione Sepharose column chromatography
-
Ni-NTA resin column chromatography and S200 HiLoad resin gel filtration
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Ni-NTA resin column chromatography, Q-Sepharose resin column chromatography, and Superdex 75 gel filtration
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Ni2+-affinity column chromatography, followed by anion exchange chromatography and gel filtration
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Ni2+-affinity column chromatography, MonoQ column chromatography, glutathione Sepharose column chromatography, Superdex 200 gel filtration, and Superdex 75 gel filtration
recombinant C-terminally His-tagged forms of enzyme domains GacSD1, GacSH1D1, GacSH2, and GacSH2H->Q from Escherichia coli strain BTH101 by nickel affinity chromatography
recombinant C-terminally His-tagged forms of enzyme domains LadSH1D1, LadSH1D1D->A, and LadSD1 from Escherichia coli strain BTH101 by nickel affinity chromatography
recombinant C-terminally poly-His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and desalting gel filtration. Overexpression of te GST-tagged enzyme in a bait and prey two hybrid system in Saccharomyces cerevisiae
recombinant CBD-tagged enzyme from Escherichia coli strain BL21(DE3) by chitin affinity chromatography with DTT thiol-induced cleavage and gel filtration to over 95% purity
recombinant FrzE protein is overproduced in Escherichia coli and purified from inclusion bodies
recombinant GST-tagged extracellular sensing domain proteins from Escherichia coli strain BL21 by glutathione affinity chromatography, tag cleavage by thrombin
recombinant His-tagged 1-121 and truncated DELTA7 H-NOXA domains from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged enzyme KinC from Escherichia coli strain BL21(DE3) by nicke affinity chromatography
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recombinant His-tagged LOVHK from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged truncated enzyme from Escherichia coli strain C43(DE3) membranes by ultracentrifugation and affinity chromatography, followed by gel filtration
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recombinant His-tagged wild-type enzyme, enzyme fragments, and mutant C70A enzyme from Escherichia coli strain Rosetta(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant His10-tagged full-length wild-type Ppr from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His6-tagged BA2291 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged extracellular sensory domain of DraK from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain M15/pREP4 by nickel affinity chromatography, dialysis, and gel filtration
recombinant protein, 1% (w/v) FosCholine-16 is most efficient in solubilizing the recombinant histidine kinase from the bacterial membranes
recombinant selenomethionine-labeled DctB residues 28-286 from Escherichia coli strain BL21(DE3) by anion exchange chromatography and gel filtration, followed by a second step of anion exchange chromatography
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recombinant selenomethionine-labeled GST-tagged DcuS residues 42-181 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography and gel filtration
recombinant wild-type and mutant enzyme domains from Escherichia coli strain BL21(DE3) by ultracentrifugation, nickel affinity chromatography, dialysis, and gel filtration
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recombinant wild-type and mutant His-tagged enzymes from Escherichia coli strain BL21(DE3) by ultracentrifugation, nickel affinity chromatography, and dialysis. His-tag removal by tobacco etch virus protease is followed by nickel affinity chromatography and gel filtration
HiTrap Ni2+-chelating column chromatography, Mono Q column chromatography, and Superdex 75 gel filtration
HiTrap Ni2+-chelating column chromatography, Mono Q column chromatography, and Superdex 75 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AaHSK1 DNA and amino acid sequence determination and analysis, cloning from strain EV-MIL31
cloned from a Salmonella typhi Ty2 cosmid bank and characterized by DNA sequence analysis
cloning of gene AlHK1 from 19 different isolates, DNA and amino acid sequence determination and analysis, sequence comparisons
cloning of the extracellular sensory domain of DraK, consisting of 88 residues (Glu28-Arg115) from genomic DNA, and overexpression as N-terminally His6-tagged protein in Escherichia coli strain BL21(DE3)
cytoplasmic expression of TorSS as a fusion protein, containing a hexahistidine tag on the N-terminus separated by a separated by a thrombin protease recognition sequence, in Escherichia coli BL21(DE3) cells
downstream of a histidine tag into vector pET15b, His-tagged full-length RaxH and RaxR overexpressed in Escherichia coli BL21 cells in the presence of sorbitol and glycine betaine to produce soluble His-RaxH
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ectopic CKI1 expression in all nuclei of the female gametophyte, under the pAKV promoter using the pOp/LhG4 transactivation system, generates non-propagating seeds with dual fertilized endosperms and no embryos, phenotypes, detailed overview
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Escherichia coli BL21(DE3) cells transformed with different pASK-IBA7-mtrB strep derivatives
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strains BL21(DE3), C41 (DE3), and C43 (DE3)
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expression in Escherichia coli
expression of Hik1 can confer fungicide-sensitivity to Saccharomyces cerevisiae. This requires both the histidine kinase and the response response regulator domain of Hik1
expression of His-tagged 1-121 and truncated DELTA7 H-NOXA domains in Escherichia coli strain BL21(DE3)
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expression of His10-tagged full-length wild-type Ppr in Escherichia coli strain BL21(DE3), overexpression of the PYP domain of Ppr in Escherichia coli, co-expression of the full-length enzyme with tyrosine ammonia-lyase and p-coumaric acid ligase
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expression of residues 10-117 of KinA, fused to an N-terminal His6Gbeta1-tag and a TEV protease site in the tag-protein linker, in Escherichia coli strain BL21(DE3), expresssion of the selenomethionine variant in Escherichia coli strain B834
expression of selenomethionine-labeled DctB residues 28-286 in Escherichia coli strain BL21(DE3)
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expression of selenomethionine-labeled DcuS residues 42-181 in Escherichia coli strain BL21(DE3) as GST-tagged protein
expression of the periplasmic domain of histidine kinase EnvZ(Ala38-Arg162) in Escherichia coli
-
expression of these proteins from a multicopy plasmid vector in Escherichia coli
Expression of wild-type and RoxRS mutant strain EU58 (mutant of two-component system) in Escherichia coli
expresssion of GST-tagged wild-type and mutant enzymes, quantitative expression analysis, overview
gene agrC, recombinant overexpression of His-tagged and GFP-tagged truncated enzyme from pET-28a-AgrCTM5-6C or pET-28-AgrCTM5-6C-GFP vector in Escherichia coli strain C43(DE3)
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gene ahk5, transient expression of GST-tagged full-length AHK5 in Arabidopsis thaliana protoplasts and Nicotiana benthamiana leaf cells the fusion protein in the cytoplasm, independent of whether the GFP tag is fused to the N-terminus or C-terminus of AHK5, expression profile of AHK5 in different tissues and cell types by semi-quantitative RT-PCR
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gene BA2291, genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay. Expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene BAB2_0652, recombinant expression f the enzyme in a two-hybrid system with PdhS in frame with the lambdacl gene, coexpression with gene pdhS, recombinant expression of His-tagged lovhk and hk domains in Escherichia coli strain BL21(DE3) pLysS from pET24a plasmid, coexpression of phyR and lovR. Antibiotic resistance complementation assays with the enzyme in Escherichia coli, overview. Realtime quantitative RT-PCR expression analysis
gene CC_0285, recombinant expression of His-tagged wild-type enzyme, enzyme fragments, and mutant C70A enzyme in Escherichia coli strain Rosetta(DE3)pLysS
gene covS, dNA and amino acid sequence determination and analysis
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gene cusS, recombinant expression of the enzyme's periplasmic domain from pTXB3CusSs plasmid, encoding CusS amino acids 39-187 with a chitin binding domain (CBD) affinity tag, in Escherichia coli strain BL21(DE3)
gene desK, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain M15/pREP4
gene fimS, DNA and amino acid sequence determination and analysis, the transcriptional start site of fimS is disrupted in strain W83
gene hik33, the chimeric gene for Hik33n-SphSc, integrated into the chromosomes, is expressed in Synechocystis from the original promoter of the sphS gene, and the copy number of each chimeric gene is exactly one per chromosome, subcloning in Escherichia coli strain JM109. Quantitative expression analysis of unaltered Hik33n-SphSc chimera and mutants under non-stressed conditions and salt-stressed conditions, overview
gene kinD, recombinant expression of the chimeric KinD-DegS hybrid kinase under control of the kinD native promoter in Escherichia coli strain DH5alpha, construct transfection to Bacillus subtilis strain NCIB3610 by SPP1 phage transduction
gene PGN_0904 or fimS, DNA and amino acid sequence determination and analysis, recombinant expression in the enzyme-deficient Porphyromonas gingivalis strain W38, complementation of the fimS variant in trans, strain ATCC 33277 FimS-induced W83 FimA is a mature polypeptide and is localized on the cell surface
gene SCO3062, recombinant expression of N-terminally GST-tagged extracellular sensing domain (residues 28E-124R), and cytoplasmic domain (residues 146R-424R) of DraK in Escherichia coli strain BL21. Because the extracellular sensing domain of DraK is sensitive to proteolysis during purification, the C-terminal truncated short form (residues 28E-115R) is also constructed without the unstable C-terminal sequence (residues 116S-124R) after determination of the cleavage site (residues 115R-116S) in the extracellular sensing domain
gene senS, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain XL-1 Blue
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gene slr1147, recombinant expression of C-terminally poly-His-tagged full-length enzyme in Escherichia coli strain BL21(DE3)
gene sphS, the chimeric gene for Hik33n-SphSc, integrated into the chromosomes, is expressed in Synechocystis from the original promoter of the sphS gene, and the copy number of each chimeric gene is exactly one per chromosome, subcloning in Escherichia coli strain JM109. Quantitative expression analysis of unaltered Hik33n-SphSc chimera and mutants under non-stressed conditions and salt-stressed conditions, overview
gene SS1G_12694, DNa and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis
gene yycG, recombinant expression of trncated enzyme mutants. Expression of a soluble cytoplasmic YycG construct in a bacterial two-hybrid expression system using the full-length YycG or a truncated YycGDELTA211-611 that lacks all cytoplasmic domains, and cell division proteins FtsZ, FtsA, FtsW, DivIB, DivIC, FtsL, Pbp2B, EzrA, ZapA, SepF and MinJ as C-terminal fusions to the individual domains (T18 and T25) of the two-domain Bordatella pertussis adenylate cyclase protein. YycG makes specific interactions with FtsL, DivIB, Pbp2B and interactions with FtsW and EzrA appear also possible
gene yycG, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3), the SeMet-substituted YycG is produced in Escherichia coli methionine auxotrophic strain B834(DE3)
genes phkA, tcsB, nikA, fphA, hk-8-2, and hk-8-5, expression of GFP-tagged enzyme in Aspergillus nidulans strain ABPU1 under the control of an HK promoter, subcloning in Escherichia coli strain JM109, analysis of the temporally and spatially different expression during the cell cycle, overview
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heterologous expression of the plnABCD operon in a Lactobacillus sake strain
into vector pGEM-T, then cloned genes disrupted in HP0244, HP1364, and HP0165 sequences. The resulting plasmids, which are unable to replicate in Helicobacter pylori, introduced into Helicobacter pylori J99
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kanamycin cartridges are inserted into the cloned fixL gene and recombined into the host genome
LOV-HK expressed in Escherichia coli
low-copy plasmid pRH324 expressing Brucella abortus pdhS fused to cfp into Sinorhizobium meliloti or Caulobacter crescentus
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overexpression of a 36-kDa truncated EnvZ protein, Glu106 to Gly450, that forms inclusion bodies in the cell
overexpression of nonreceptor-type HK gene cytokinin independent1 (CKI1) activates cytokinin signaling, quantitative RT-PCR expression analysis
pBOS1delta linearized and used to transform protoplasts of the UWS111 wild-type strain
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profiling of a HP0244 deletion mutant grown at pH 7.4, contribution of HP0244 to sigma(54) activation via HP0703 to coordinate flagellar biosynthesis by a pH-independent regulon that includes 14 flagellar genes. Microarray analysis of cells grown at pH 4.5 without urea reveals an additional 22 genes, including 4 acid acclimation genes, e.g. ureA, ureB, ureI, and amiE, that are positively regulated by HP0244, overview
recombinant expression of C-terminally His-tagged forms of enzyme domains GacSD1, GacSH1D1, GacSH2, and GacSH2H->Q in Escherichia coli strain BTH101, expression of N-terminally FLAG or Strep tagged enzyme fragment constructs
recombinant expression of C-terminally His-tagged forms of enzyme domains LadSH1D1, LadSH1D1D->A, and LadSD1 in Escherichia coli strain BTH101, expression of N-terminally FLAG or Strep tagged enzyme fragment constructs
recombinant expression of His-tagged enzyme KinC in Escherichia coli strain BL21(DE3)
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recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli. The expression of CusS from a plasmid does not result in the same growth phenotype on copper-containing media as the strain that expresses chromosomal CusS
recombinant expression of wild-type and mutant enzyme domains in Escherichia coli strain BL21(DE3)
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli
the sensing GAF domain of DosT is expressed in Escherichia coli BL21gold DE3 cells
wild-type and mutants introduced into deltarodK strain SA1708, His6-tagged wild-type and mutants expressed in Escherichia coli
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cytoplasmic expression of TorSS as a fusion protein, containing a hexahistidine tag on the N-terminus separated by a separated by a thrombin protease recognition sequence, in Escherichia coli BL21(DE3) cells
cytoplasmic expression of TorSS as a fusion protein, containing a hexahistidine tag on the N-terminus separated by a separated by a thrombin protease recognition sequence, in Escherichia coli BL21(DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
2.5fold enhanced transcription of SaeS after incubation with Perform and SDS
during Anaplasma phagocytophilum development in human promyelocytic HL-60 cells, PleC is downregulated prior to extracellular release
during Anaplasma phagocytophilum development in human promyelocytic HL-60 cells, PleC is upregulated at the exponential growth stage
HhkA is actively transcribed during sporangium formation and dehiscence
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histidine kinase mRNA accumulation is induced by 140 mM acetosyringone
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PhoQ is activated by acidic pH (pH 5.5)
promoters of fphA, hk-8-2, and hk-8-5 preferentially function in conidial heads, the promoter of phkA preferentially functions in cleistothecia, and the promoters of tcsB and nikA function in both conidial heads and cleistothecia
2.5fold enhanced transcription of SaeS after incubation with Perform and SDS
2.5fold enhanced transcription of SaeS after incubation with Perform and SDS
-
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PhoQ is activated by acidic pH (pH 5.5)
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promoters of fphA, hk-8-2, and hk-8-5 preferentially function in conidial heads, the promoter of phkA preferentially functions in cleistothecia, and the promoters of tcsB and nikA function in both conidial heads and cleistothecia
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promoters of fphA, hk-8-2, and hk-8-5 preferentially function in conidial heads, the promoter of phkA preferentially functions in cleistothecia, and the promoters of tcsB and nikA function in both conidial heads and cleistothecia
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
chemical reconstitution of the recombinantly expressed PYP domain of Ppr with 4-coumaric acid
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protein refolding is achieved by dialysis in storage buffer (50 mM Tris-HCl pH 7.6, 0.5 mM dithiothreitol, 50% (v/v) glycerol) containing 0.01% (v/v) Triton X-100
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purified recombinant truncated enzyme proteins are reconstituted into liposomes by a detergent-mediated method, effect of different detergents on protein reconstitution efficiency, overview. The highest incorporation is found with N,N-dimethyldode-cylamine N-oxide resulting in a yield of 85%, liposomes are consisting of dioleoyl-phosphatidyl-choline : 1,2-dipalmitoyl-sn-glycero-3-phosphocholine : egg L-alpha-phosphatidic acid : cholesterol at molar ratios of 4:4:1:1, pH 7.4. Determination of the morphology and size of liposome, overview
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the refolded recombinant protein is obtained by gradual removal of 6 M urea by sequential dialysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
additional information
medicine
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significance in pathological virulence of Salmonella enterica, seductive target for anti-bacterial therapeutic development
medicine
NME1 expression is associated with reduced overall and event-free survival of neuroblastoma patients and with the strongest associations of any of the NME family member genes. NME1 expression is also higher in tumors with MYCN oncogene amplification and in tumors from patients with stage 4 disease. Isoforms NME1/NMe2 and multiple phosphorylated His-containing proteins are found in all tested neuroblastoma cell lines and in xenograft neuroblastoma tumors. NME1 expression is asssociated with neuroblastoma cell migration and differentiation
synthesis
the deletion of histidine kinases cbei2073 and cbei4484 results in significant change in butanol biosynthesis, with butanol production increased by 40.8 and 17.3% (13.8 g/L and 11.5 g/L vs. 9.8 g/L), respectively, compared to the wild-type. Faster butanol production rates are observed, with butanol productivity greatly increased by 40.0 and 20.0%, respectively. The sporulation frequencies of two histidine kinases inactivated strains decrease by 96.9 and 77.4%, respectively
synthesis
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the deletion of histidine kinases cbei2073 and cbei4484 results in significant change in butanol biosynthesis, with butanol production increased by 40.8 and 17.3% (13.8 g/L and 11.5 g/L vs. 9.8 g/L), respectively, compared to the wild-type. Faster butanol production rates are observed, with butanol productivity greatly increased by 40.0 and 20.0%, respectively. The sporulation frequencies of two histidine kinases inactivated strains decrease by 96.9 and 77.4%, respectively
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additional information
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Hik33, Hik34, Hik16 and Hik41, are involved in perception and transduction of H2O2 signals that regulate the gene expression of 26 of the 77 H2O2-inducible genes with induction factors higher than 4.0, Hik33 is the main contributor
additional information
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15 of the 30 known Escherichia coli histidine kinases contain a single HAMP domain, has an important role in signal transduction
additional information
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intact HP0165 and HP1364 histidine kinases are required for acid resistance in Helicobacter pylori
additional information
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44 genes for Hiks on the chromosome, Hik34 might act as a negative regulator of the expression of heat-shock genes during normal growth. Hik33 is a cold sensor, participates in the positive regulation of the expression of more than 60% of the cold-inducible genes, is also involved in the perception of hyperosmotic stress and salt stress and transduction of the signals, findings cannot be explained by the current model of two-component systems
additional information
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hybrid histidine protein kinase in which four signalling domains are required for full activity
additional information
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BOS1 is necessary for normal osmoregulation, is not the general oxidative stress signal transducer, is required for normal macroconidiation and full virulence
additional information
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PdhS contains an N-terminal multimerization part and a C-terminal histidine kinase part interacting with DivK, PdhS can enhance the phosphorylation of DivK and its subsequent polar localization, the enzyme has essential functions in controlling some aspects of the division process, maybe through the control of CtrA activity, PdhS recognizes a polar structure conserved in several alpha-proteobacteria
additional information
responsible role of the response regulator TrrA for the feedback regulation of sensing and/or kinase activities of ThkA
additional information
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responsible role of the response regulator TrrA for the feedback regulation of sensing and/or kinase activities of ThkA
additional information
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MtrB belongs to a class of histidine protein kinases that sense environmental changes at cytoplasmatic protein domains independently of the periplasmic loop and the cytoplasmic HAMP domain
additional information
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great effect of temperature on the dynamics of the HAMP linker domain, which is a key feature in signal transduction
additional information
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induces phosphorylation of its concomitant response regulator RaxR
additional information
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a LOV domain at the N-terminus, followed by a PAS domain in the intervening sequence, and a histidine kinase at the C-terminus
additional information
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a LOV domain at the N-terminus, followed by a PAS domain in the intervening sequence, and a histidine kinase at the C-terminus
additional information
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LOV domain followed by a linking sequence and a C-terminal histidine kinase domain
additional information
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LOV domain at the N terminus, followed by a histidine kinase and a putative C-terminal receiver domain
additional information
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long-range signal transmission through the histidine kinase VirA can be exploited for synthetic signaling circuits
additional information
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great effect of temperature on the dynamics of the HAMP linker domain, which is a key feature in signal transduction
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additional information
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LOV domain at the N terminus, followed by a histidine kinase and a putative C-terminal receiver domain
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additional information
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BOS1 is necessary for normal osmoregulation, is not the general oxidative stress signal transducer, is required for normal macroconidiation and full virulence
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additional information
-
PdhS contains an N-terminal multimerization part and a C-terminal histidine kinase part interacting with DivK, PdhS can enhance the phosphorylation of DivK and its subsequent polar localization, the enzyme has essential functions in controlling some aspects of the division process, maybe through the control of CtrA activity, PdhS recognizes a polar structure conserved in several alpha-proteobacteria
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additional information
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induces phosphorylation of its concomitant response regulator RaxR
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additional information
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long-range signal transmission through the histidine kinase VirA can be exploited for synthetic signaling circuits
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EXTERNAL LINKS (specific for EC-Number 2.7.13.3)
Transporter Classification Database (TCDB): 9.B.33.1.1, 9.B.238.3.5, 9.B.33.1.2, 2.A.21.9.1, 2.A.21.9.2, 2.A.123.2.13
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Release 2026.1 (March 2026)
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