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Information on EC 2.7.10.3 - bacterial tyrosine kinase
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EC Tree
2.7.10.3 bacterial tyrosine kinaseIUBMB Comments
This family of enzymes includes most of the bacterial tyrosine kinases. These enzymes do not share sequence or structural homology with eukaryotic tyrosine kinases, and exploit ATP/GTP-binding Walker motifs to catalyse autophosphorylation and substrate phosphorylation on tyrosine. Two subfamilies have been defined: P-type enzymes contain an N-terminal transmembrane portion and an extracellular hairpin loop domain. The intracellular portion comprises the catalytic domain and a tyrosine-rich C-terminal domain that contains the site for autophosphorylation. In F-type enzymes the extracellular transmembrane domain and the intracellular catalytic domain are two independent proteins encoded by two separate genes. The majority of characterized bacterial tyrosine kinases regulate the production and export of capsular and extracellular polysaccharides, but other members are involved in many other functions.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
src protein kinase, by-kinase, capb2, bacterial tyrosine kinase, cap5b2, sll0923, bacterial protein tyrosine kinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bacterial protein tyrosine kinase
-
-
-
-
BtkA
BtkB
BY-kinase
DivL
MXAN_1025
MXAN_3228
PGN_1524
PTK1
Wzc
BY-kinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:[protein]-L-tyrosine O-phosphotransferase (bacterial-type)
This family of enzymes includes most of the bacterial tyrosine kinases. These enzymes do not share sequence or structural homology with eukaryotic tyrosine kinases, and exploit ATP/GTP-binding Walker motifs to catalyse autophosphorylation and substrate phosphorylation on tyrosine. Two subfamilies have been defined: P-type enzymes contain an N-terminal transmembrane portion and an extracellular hairpin loop domain. The intracellular portion comprises the catalytic domain and a tyrosine-rich C-terminal domain that contains the site for autophosphorylation. In F-type enzymes the extracellular transmembrane domain and the intracellular catalytic domain are two independent proteins encoded by two separate genes. The majority of characterized bacterial tyrosine kinases regulate the production and export of capsular and extracellular polysaccharides, but other members are involved in many other functions.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-tyrosyl-[AAVHEYLSA]
ADP + H+ + O-phospho-L-tyrosyl-[AAVHEYLSA]
AAVHEYLSA i.e. peptide derived from the tyrosine-rich BceF C-terminal region containing the third distal tyrosine only (733AAVHEYLSA741)
-
-
?
ATP + L-tyrosyl-[CapB2]
ADP + H+ + O-phospho-L-tyrosyl-[CapB2]
-
-
-
?
ATP + L-tyrosyl-[CpsD]
ADP + H+ + O-phospho-L-tyrosyl-[CpsD]
-
-
-
-
?
ATP + L-tyrosyl-[ParB]
ADP + H+ + O-phospho-L-tyrosyl-[ParB]
-
substrate is chromosome segregation protein ParB. CpsD interacts with ParB and phosphorylation modulates the mobility of ParB
-
-
?
ATP + L-tyrosyl-[PTK]
ADP + H+ + O-phospho-L-tyrosyl-[PTK]
-
-
-
?
ATP + L-tyrosyl-[Wzc]
ADP + H+ + O-phospho-L-tyrosyl-[Wzc]
-
-
-
?
ATP + [chain length determinant family protein Exo]-L-tyrosine
ADP + [chain length determinant family protein Exo]-L-tyrosine phosphate
ATP + L-Tyr550-[DivL]
ADP + H+ + O-phospho-L-Tyr550-[DivL]
-
-
-
?
ATP + L-Tyr550-[DivL]
ADP + H+ + O-phospho-L-Tyr550-[DivL]
-
-
-
?
ATP + L-tyrosine in poly(Glu,Tyr)
ADP + H+ + O-phospho-L-tyrosyl-poly(Glu,Tyr)
poly(Glu, Tyr; 4:1), used as universal substrate for protein tyrosine kinases
-
-
?
ATP + L-tyrosine in poly(Glu,Tyr)
ADP + H+ + O-phospho-L-tyrosyl-poly(Glu,Tyr)
poly(Glu, Tyr; 4:1), used as universal substrate for protein tyrosine kinases
-
-
?
ATP + L-tyrosyl-[BtkB]
ADP + H+ + O-phospho-L-tyrosyl-[BtkB]
-
-
-
?
ATP + L-tyrosyl-[BtkB]
ADP + H+ + O-phospho-L-tyrosyl-[BtkB]
-
-
-
?
ATP + L-tyrosyl-[CtrA]
ADP + H+ + O-phospho-L-tyrosyl-[CtrA]
-
-
-
?
ATP + L-tyrosyl-[CtrA]
ADP + H+ + O-phospho-L-tyrosyl-[CtrA]
-
-
-
?
ATP + L-tyrosyl-[PGN_0224]
ADP + H+ + O-phospho-L-tyrosyl-[PGN_0224]
substrate is UDP-acetyl-mannosamine dehydrogenase, a capsule related protein
-
-
?
ATP + L-tyrosyl-[PGN_0224]
ADP + H+ + O-phospho-L-tyrosyl-[PGN_0224]
substrate is UDP-acetyl-mannosamine dehydrogenase, a capsule related protein
-
-
?
ATP + L-tyrosyl-[PGN_0613]
ADP + H+ + O-phospho-L-tyrosyl-[PGN_0613]
substrate is UDP-glucose dehydrogenase, a capsule related protein
-
-
?
ATP + L-tyrosyl-[PGN_0613]
ADP + H+ + O-phospho-L-tyrosyl-[PGN_0613]
substrate is UDP-glucose dehydrogenase, a capsule related protein
-
-
?
ATP + L-tyrosyl-[PTK1]
ADP + H+ + O-phospho-L-tyrosyl-[PTK1]
-
-
-
?
ATP + L-tyrosyl-[PTK1]
ADP + H+ + O-phospho-L-tyrosyl-[PTK1]
-
-
-
?
ATP + [BtkA]-L-tyrosine
ADP + [BtkA]-L-tyrosine phosphate
-
-
-
?
ATP + [chain length determinant family protein Exo]-L-tyrosine
ADP + [chain length determinant family protein Exo]-L-tyrosine phosphate
-
-
-
?
ATP + [chain length determinant family protein Exo]-L-tyrosine
ADP + [chain length determinant family protein Exo]-L-tyrosine phosphate
-
-
-
?
ATP + [myelin]-L-tyrosine
ADP + [myelin]-L-tyrosine phosphate
-
-
-
?
ATP + [myelin]-L-tyrosine
ADP + [myelin]-L-tyrosine phosphate
-
-
-
?
additional information
?
-
no phosphorylation of synthetic substrates such as poly(Glu80 Tyr20) or angiotensin II is observed
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-
-
additional information
?
-
no substrate: response regulator DivK
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-
-
additional information
?
-
-
no substrate: response regulator DivK
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-
-
additional information
?
-
no substrate: response regulator DivK
-
-
-
additional information
?
-
no substrate: synthetic peptide RRLIEDADYAARG
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-
-
additional information
?
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-
no substrate: synthetic peptide RRLIEDADYAARG
-
-
-
additional information
?
-
no substrate: synthetic peptide RRLIEDADYAARG
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
Mn2+ or Co2+ are not able to substitute for Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine
0.2 mM, 64% inhibition
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
Src protein kinase pp60c-src influences adhesion stabilization of HT-29 colon carcinoma cells to extracellular matrix components under dynamic conditions of laminar flow.
Colorectal Neoplasms
Curcumin Enhances the Effect of Chemotherapy against Colorectal Cancer Cells by Inhibition of NF-?B and Src Protein Kinase Signaling Pathways.
Cystic Fibrosis
Structural and Functional Insights into the Biofilm-Associated BceF Tyrosine Kinase Domain from Burkholderia cepacia.
Infections
Lyn is involved in host defense against S. agalactiae infection and BCR signaling in Nile tilapia (Oreochromis niloticus).
Neoplasms
Dasatinib attenuates overexpression of Src signaling induced by the combination treatment of veliparib plus carboplatin in triple-negative breast cancer.
Papilloma
The prostaglandin receptor EP2 activates multiple signaling pathways and beta-arrestin1 complex formation during mouse skin papilloma development.
Prostatic Neoplasms
Re: Ligand-dependent corepressor acts as a novel androgen receptor corepressor, inhibits prostate cancer growth, and is functionally inactivated by the Src protein kinase.
Respiratory Tract Infections
Structural and Functional Insights into the Biofilm-Associated BceF Tyrosine Kinase Domain from Burkholderia cepacia.
Sarcoma, Avian
Association of pp60src and src protein kinase activity with the plasma membrane of nonpermissive and permissive avian sarcoma virus-infected cells.
Sarcoma, Avian
Downregulation of cell-to-cell communication by the viral src gene is blocked by TMB-8 and recovery of communication is blocked by vanadate.
Whooping Cough
Receptor-type protein tyrosine phosphatase zeta as a component of the signaling receptor complex for midkine-dependent survival of embryonic neurons.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
L-tyrosine in poly(Glu,Tyr)
Km value 0.3 mg/ml, cytoplasmic fragment of BtkB (Ser444-Ser710), pH 7, 37°C
-
additional information
L-tyrosine in poly(Glu,Tyr)
-
Km value 0.3 mg/ml, cytoplasmic fragment of BtkB (Ser444-Ser710), pH 7, 37°C
-
additional information
L-tyrosine in poly(Glu,Tyr)
Km value 0.375 mg/ml, mutant Y686F/Y690F/Y693F/Y696F/Y699F, pH 7, 37°C
-
additional information
L-tyrosine in poly(Glu,Tyr)
-
Km value 0.375 mg/ml, mutant Y686F/Y690F/Y693F/Y696F/Y699F, pH 7, 37°C
-
additional information
L-tyrosine in poly(Glu,Tyr)
Km value 1.35 mg/ml, mutant R550Y, pH 7, 37°C
-
additional information
L-tyrosine in poly(Glu,Tyr)
-
Km value 1.35 mg/ml, mutant R550Y, pH 7, 37°C
-
additional information
polyE4Y
Km value 105 microg/ml, wild-type, pH 8, 30°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0002
L-tyrosine in poly(Glu,Tyr)
mutant Y686F/Y690F/Y693F/Y696F/Y699F, pH 7, 37°C
-
0.0003
L-tyrosine in poly(Glu,Tyr)
cytoplasmic fragment of BtkB (Ser444-Ser710), pH 7, 37°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
-
identification of BY-kinase sequences in UniProt Knowledgebase using a combination of similarity search with sequence-profile alignment, pattern matching and sliding window computation. The sequence is distinct from other protein families by the presence of three specific Walker-like motifs (one Walker-A-like followed by two Walker-B-like) and a YC. The BY-kinase family signature is summarized as a PROSITE pattern: G-K-[ST]-X(7,27)-[ILVFM](3)-D-X-D-X-RX(60,80)-[ILVFM](3)-D-X(2)-P-X(30,150)-Y-X(0,5)-Y, leading to identification of 640 sequences
metabolism
phosphorylating capacity of Cap5B2 is expressed only in the presence of a stimulatory protein, either Cap5A1 or Cap5A2, that enhances its affinity for the phosphoryl donor ATP. The last 27/29 amino acids of the C-terminal domain of either polypeptide are sufficient for stimulating Cap5B2 activity
metabolism
PTK1 can utilize ATP for autophosphorylation and is dephosphorylated by the tyrosine phosphatase, Ltp1
metabolism
regulatory interaction of tyrosine kinase Wzc, and its opposing tyrosine phosphatase, Wzb. The phosphatase Wzb utilizes a surface distal to the catalytic elements of the kinase, Wzc, to dock onto its catalytic domain WzcCD. WzcCD binds in a fashion largely independent of the C-terminal tyrosine cluster near the Wzb catalytic site, inducing allosteric changes therein. YC dephosphorylation is proximity-mediated and reliant on the elevated concentration of phosphorylated YC near the Wzb active site resulting from WzcCD docking
metabolism
the conformation of the Walker-A lysine is coupled to the global transitions of the cytoplasmic catalytic domain. Global closure drives ATP toward its reactive conformation, while active site ordering promotes the desolvation of ATP. The closed state is stabilized in the octameric ring with characteristic ATP conformations
metabolism
-
PTK1 can utilize ATP for autophosphorylation and is dephosphorylated by the tyrosine phosphatase, Ltp1
-
physiological function
a BtkA mutant is unable to complete maturation to heat- and sonication-resistant spores under both starvation- and glycerol-induced developmental conditions
physiological function
a BtkB mutant shows reduced maximum cell density as compared to the wild type when cultured in nutrient medium at 37°C. Under starvation conditions, BtkB mutant cells form fruiting bodies and spores about 24 h later than the wild-type strain. The BtkB mutant overproduces yellow pigment during development and shows a decrease in exopolysaccharide production when compared with the wild-type strain
physiological function
autophosphorylation of Wzc is essential for assembly of the serotype K30 group 1 capsule in Escherichia coli O9a:K30. It is not essential for either the synthesis of the K30 repeat units or for activity of the K30 polymerase enzyme. The tyrosine-rich domain at the C terminus of Wzc is the site of phosphorylation, and autophosphorylation of Wzc requires a functional Walker A motif. The N- and C-terminal domains of Wzc are both required for phosphorylation of the Wzc C terminus, and for capsule assembly
physiological function
-
BY-kinase CpsD and capsular polysaccharide biosynthesis protein CpsC are required for growth in Streptococcus pneumoniae. CpsD autokinase activity is dispensable for growth, but autophosphorylation modulates the length of the capsular polysaccharides. Cells lacking a functional CpsC or cpsD accumulate low molecular weight capsular polysaccharide and lyse because of the lethal sequestration of the lipid carrier undecaprenyl phosphate, resulting in inhibition of peptidoglycan synthesis. CpsC interacts with CpsD and the polymerase CpsH. CpsD phosphorylation reduces the length of capsular polysaccharide polymers presumably by controlling the activity of CpsC. The spatiotemporal coordination between capsular polysaccharide and peptidoglycan synthesis is dependent on CpsC and CpsD
physiological function
-
CpsD localizes at the cell division site and participates in the proper assembly of the capsule. The cytoplasmic C-terminal end of the transmembrane protein CpsC is required for CpsD autophosphorylation and localization at mid-cell. The CpsC/CpsD complex captures the polysaccharide polymerase CpsH at the division site and CPS production occurs exclusively at mid-cell and is tightly dependent on CpsD interaction with CpsC. Non-phosphorylated CpsD hinders capsule production and cell division, septal localization of non-phosphorylated CpsD impairs cell division
physiological function
DivL is autophosphorylated on residue Tyr550 in vitro, and this tyrosine residue is essential for cell viability and regulation of the cell division cycle. DivL in vitro catalyzes phosphorylation of global response regulator CtrA and activates transcription in vitro of the cell cycle-regulated FliF promoter
physiological function
in a PTK1 mutant,community development with Streptococcus gordonii is severely abrogated. Ptk1 controls the levels of the transcriptional regulator CdhR and the fimbrial adhesin Mfa1 which mediates binding to Streptococcus gordonii. The PTK1 gene is in an operon with two genes involved in exopolysaccharide synthesis, and Ptk1 is necessary for exopolysaccharide production in Porphyromonas gingivalis. Knockout of PTK1 in an encapsulated strain of Porphyromonas gingivalis results in loss of capsule production
physiological function
protein tyrosine kinase Wzc participates in the production of capsular (CPS) and released (RPS) polysaccharides. The phosphorylation state of Wzc is dependent on the activity of phosphatase Wzb. The absence of phosphatase Wzb affects the phosphorylation/dephosphorylation cycles of Wzc, altering released polysaccharides production, and this effect is not replicated when the Y-rich region of Wzc is truncated
physiological function
-
DivL is autophosphorylated on residue Tyr550 in vitro, and this tyrosine residue is essential for cell viability and regulation of the cell division cycle. DivL in vitro catalyzes phosphorylation of global response regulator CtrA and activates transcription in vitro of the cell cycle-regulated FliF promoter
-
physiological function
-
in a PTK1 mutant,community development with Streptococcus gordonii is severely abrogated. Ptk1 controls the levels of the transcriptional regulator CdhR and the fimbrial adhesin Mfa1 which mediates binding to Streptococcus gordonii. The PTK1 gene is in an operon with two genes involved in exopolysaccharide synthesis, and Ptk1 is necessary for exopolysaccharide production in Porphyromonas gingivalis. Knockout of PTK1 in an encapsulated strain of Porphyromonas gingivalis results in loss of capsule production
-
physiological function
-
a BtkA mutant is unable to complete maturation to heat- and sonication-resistant spores under both starvation- and glycerol-induced developmental conditions
-
physiological function
-
a BtkB mutant shows reduced maximum cell density as compared to the wild type when cultured in nutrient medium at 37°C. Under starvation conditions, BtkB mutant cells form fruiting bodies and spores about 24 h later than the wild-type strain. The BtkB mutant overproduces yellow pigment during development and shows a decrease in exopolysaccharide production when compared with the wild-type strain
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). B2RKZ8_PORG3
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
821
0
92715
TrEMBL
-
SRC_CHICK
533
0
60010
Swiss-Prot
Mitochondrion (Reliability: 2)
P72877_SYNY3
Synechocystis sp. (strain PCC 6803 / Kazusa)
756
0
83641
TrEMBL
other Location (Reliability: 2)
Q0GYW2_BURCE
741
0
79598
TrEMBL
other Location (Reliability: 4)
DIVL_CAUVC
Caulobacter vibrioides (strain ATCC 19089 / CB15)
769
1
82796
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 78400, calculated from sequence, x * 82000, SDS-PAGE of recombinant protein
?
-
x * 78400, calculated from sequence, x * 82000, SDS-PAGE of recombinant protein
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
presence of at least five isoforms, all phosphorylated exclusively at tyrosine. Autophosphorylation occurs at multiple sites within the protein
phosphoprotein
DivL contains a tyrosine residue (Tyr550) in the conserved H-box instead of a histidine residue, which is the expected site of autophosphorylation
phosphoprotein
-
DivL contains a tyrosine residue (Tyr550) in the conserved H-box instead of a histidine residue, which is the expected site of autophosphorylation
-
phosphoprotein
autophosphorylation of Wzc is essential for assembly of the serotype K30 group 1 capsule in Escherichia coli O9a:K30. It is not essential for either the synthesis of the K30 repeat units or for activity of the K30 polymerase enzyme. The tyrosine-rich domain at the C terminus of Wzc is the site of phosphorylation, and autophosphorylation of Wzc requires a functional Walker A motif. The N- and C-terminal domains of Wzc are both required for phosphorylation of the Wzc C terminus
phosphoprotein
autophosphorylation of BtkA is activated by the addition of chain length determinant family protein Exo. The reaction leads to the phosphorylation of BtkA and of Exo in a ratio of approximately 1.5:1 to 2:1
phosphoprotein
-
autophosphorylation of BtkA is activated by the addition of chain length determinant family protein Exo. The reaction leads to the phosphorylation of BtkA and of Exo in a ratio of approximately 1.5:1 to 2:1
-
phosphoprotein
chimeric CapAB protein is multiply autophosphorylated
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the BceF kinase domain at 1.85 A resolution. The isolated BceF kinase domain is assembled as a dimer in solution and crystallizes as a dimer in the asymmetric unit with endogenous adenosine-diphosphate bound at the active sites. The low enzymatic efficiency measured in solution may be explained by the partial obstruction of the active sites at the crystallographic dimer interface
monomeric Wzc catalytic domain preferentially populates states characterized by distortions at its oligomerization interfaces and by catalytic element conformations that allow high-affinity interactions with ADP but not with ATP-Mg2+. Formation of the octameric ring stabilizes the intermonomer interfaces and results in catalytic element conformations suitable for optimally engaging ATP-Mg2+, facilitating exchange with bound ADP. This sequence of events, oligomerization, i.e., substrate binding, before engaging ATP-Mg2+, facilitates optimal autophosphorylation by preventing a futile cycle of ATP hydrolysis
structure of the C-terminal kinase domain 2.5 A resolution. The fold of the Etk kinase domain differs markedly from that of eukaryotic protein tyrosine kinases. The activation mechanism proposed involves the phosphorylated Tyr residue, Y574, at the active site and its specific interaction with key Arg residue, R614, to unblock the active site
structures of the phosphorylated and unphosphorylated states of CapB2 together with the activator domain of its cognate transmembrane modulator CapA. The structure reveals a 230-kDa ring-shaped octamer that dissociates upon intermolecular autophosphorylation
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y550F
mutant is not able to complement loss of DivL activity, mutant protein is autophosphorylated weakly at a level ca. 6fold lower than that of wild-type and 6fold less active in the phosphorylation of CtrA
Y550H
mutant is not able to complement loss of DivL activity, no autophosphorylation or phosphorylation of CtrA can be detected
Y550F
-
mutant is not able to complement loss of DivL activity, mutant protein is autophosphorylated weakly at a level ca. 6fold lower than that of wild-type and 6fold less active in the phosphorylation of CtrA
-
Y550H
-
mutant is not able to complement loss of DivL activity, no autophosphorylation or phosphorylation of CtrA can be detected
-
K540M
residues K540-D642 form a salt bridge. Mutant has a measurably higher affinity for ADP-g2+ over a range of Mg2+ concentrations. In presence of Mg2+, monomeric K540M protein forms oligomers
Y569F
mutant protein leads to production of exopolysaccharides with aberrant sizes. Mutation has little effect on the conformation of bound ATP
H384A
upon recombinant expression, mutants accumulates to significant level in the insoluble fraction
H384Q
upon recombinant expression, mutants accumulates to significant level in the insoluble fraction
H384Y
mutation in a universally conserved residue among protein tyrosine kinases, residue is not essential for Src catalysis or its inactivation by C-terminal tail Tyr phosphorylation. His384 mutants undergo autophosphorylation on Tyr416 like wild-type Src but are not activated by autophosphorylation
N391D
upon recombinant expression, mutant accumulates to a predominant level in the insoluble fraction and a significant level in the soluble fraction
R388A/A390R
upon recombinant expression, mutant does not accumulate to detectable levels
R550Y
mutation reduces autophosphorylation activity by about 95% and the poly(Glu, Tyr) activity by about 91%
Y686F/Y690F/Y693F/Y696F/Y699F
R550Y
-
mutation reduces autophosphorylation activity by about 95% and the poly(Glu, Tyr) activity by about 91%
-
Y686F/Y690F/Y693F/Y696F/Y699F
additional information
Y686F/Y690F/Y693F/Y696F/Y699F
complete loss of autophosphorylation with only slightly reduced poly(Glu, Tyr) kinase activities
Y686F/Y690F/Y693F/Y696F/Y699F
mutant shows a great reduced level of autophosphorylation
Y686F/Y690F/Y693F/Y696F/Y699F
-
mutant shows a great reduced level of autophosphorylation
-
Y686F/Y690F/Y693F/Y696F/Y699F
-
complete loss of autophosphorylation with only slightly reduced poly(Glu, Tyr) kinase activities
-
additional information
a deletion mutant lacking the predicted activator domain (amino acids 444-464) loses autophosphorylation and poly(Glu, Tyr) kinase activities. A cytoplasmic fragment of BtkB (Ser444-Ser710) carrying replacments of all C-terminal tyrosine residues with phenylalanines, does not undergo autophosphorylation. This mutation does not significantly affect poly(Glu, Tyr) kinase activity. A cytoplasmic fragment of BtkB carrying mutations of the conserved motif ExxRxxR of BY kinases which is involved in the self-association of catalytic domains, leads to loss of autophosphorylation and poly(Glu, Tyr) kinase activities
additional information
-
a deletion mutant lacking the predicted activator domain (amino acids 444-464) loses autophosphorylation and poly(Glu, Tyr) kinase activities. A cytoplasmic fragment of BtkB (Ser444-Ser710) carrying replacments of all C-terminal tyrosine residues with phenylalanines, does not undergo autophosphorylation. This mutation does not significantly affect poly(Glu, Tyr) kinase activity. A cytoplasmic fragment of BtkB carrying mutations of the conserved motif ExxRxxR of BY kinases which is involved in the self-association of catalytic domains, leads to loss of autophosphorylation and poly(Glu, Tyr) kinase activities
additional information
a deletion mutant lacking the Y-cluster, amino acids 686-699, shows a great reduced level of autophosphorylation
additional information
-
a deletion mutant lacking the Y-cluster, amino acids 686-699, shows a great reduced level of autophosphorylation
additional information
-
a deletion mutant lacking the Y-cluster, amino acids 686-699, shows a great reduced level of autophosphorylation
-
additional information
-
a deletion mutant lacking the predicted activator domain (amino acids 444-464) loses autophosphorylation and poly(Glu, Tyr) kinase activities. A cytoplasmic fragment of BtkB (Ser444-Ser710) carrying replacments of all C-terminal tyrosine residues with phenylalanines, does not undergo autophosphorylation. This mutation does not significantly affect poly(Glu, Tyr) kinase activity. A cytoplasmic fragment of BtkB carrying mutations of the conserved motif ExxRxxR of BY kinases which is involved in the self-association of catalytic domains, leads to loss of autophosphorylation and poly(Glu, Tyr) kinase activities
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additional information
expression of a chimeric protein CapAB protein comprides of the Cap5A1 C-terminal fragment fused to the N-terminal extremity of Cap5B2 and of its inactive P-loop mutant CapAB K55M
additional information
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expression of a chimeric protein CapAB protein comprides of the Cap5A1 C-terminal fragment fused to the N-terminal extremity of Cap5B2 and of its inactive P-loop mutant CapAB K55M
additional information
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mutants that change the phosphorylation status of CpsD are viable but with defective CPS production.When the C-terminal tyrosine residues of CpsD are changed to nonphosphorylable phenylalanine, cells synthesize very little low molecular weight capsular polysaccharide. When the C-terminal tyrosine residues of CpsD are changed phospho-mimicking glutamate, cells synthesize significantly more low molecular weight capsular polysaccharide
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
during recombinant expression, Src activity is toxic to the bacteria, which prevents high-level expression of fully active Src. Src mutants with kinase activity above a certain threshold cannot be purified from a bacterial expression system, while a variety of mutants with a kinase activity below this threshold can indeed be expressed and purified
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
BtkA is expressed late after starvation induction and early after glycerol induction
the BtkB gene is expressed mainly in the growth phase and early stages of fruiting body development
BtkA is expressed late after starvation induction and early after glycerol induction
BtkA is expressed late after starvation induction and early after glycerol induction
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the BtkB gene is expressed mainly in the growth phase and early stages of fruiting body development
the BtkB gene is expressed mainly in the growth phase and early stages of fruiting body development
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kemble, D.J.; Wang, Y.H.; Sun, G.
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45
14749-14754
2006
Gallus gallus (P00523)
brenda
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Bacteria
brenda
Mayer, M.; Matiuhin, Y.; Nawatha, M.; Tabachnikov, O.; Fish, I.; Schutz, N.; Dvir, H.; Landau, M.
Structural and functional insights into the biofilm-associated BceF tyrosine kinase domain from Burkholderia cepacia
Biomolecules
11
1196
2021
Burkholderia cepacia (Q0GYW2), Burkholderia cepacia
brenda
Lee, D.; Zheng, J.; She, Y.; Jia, Z.
Structure of Escherichia coli tyrosine kinase Etk reveals a novel activation
EMBO J.
27
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2008
Escherichia coli (P38134)
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Kimura, Y.; Kato, T.; Mori, Y.
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FEMS Microbiol. Lett.
336
45-51
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Myxococcus xanthus (Q1DDI7), Myxococcus xanthus, Myxococcus xanthus DK1622 (Q1DDI7)
brenda
Grangeasse, C.; Doublet, P.; Vaganay, E.; Vincent, C.; Deleage, G.; Duclos, B.; Cozzone, A.J.
Characterization of a bacterial gene encoding an autophosphorylating protein tyrosine kinase
Gene
204
259-265
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Acinetobacter johnsonii (O52788)
brenda
Kimura, Y.; Yamashita, S.; Mori, Y.; Kitajima, Y.; Takegawa, K.
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193
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Myxococcus xanthus (Q1D7E6), Myxococcus xanthus, Myxococcus xanthus DK1622 (Q1D7E6)
brenda
Kato, T.; Shirakawa, Y.; Takegawa, K.; Kimura, Y.
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158
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Myxococcus xanthus (Q1DDI7), Myxococcus xanthus, Myxococcus xanthus DK1622 (Q1DDI7)
brenda
Wugeditsch,T.; Paiment, A.; Hocking,J.; Drummelsmith, J.; Forrester, C.; Whitfield, C.
Phosphorylation of Wzc, a tyrosine autokinase, is essential for assembly of group 1 capsular polysaccharides in Escherichia coli
J. Biol. Chem.
276
2361-2371
2001
Escherichia coli (Q9X4B9)
brenda
Soulat, D.; Jault, J.; Duclos, B.; Geourjon, C.; Cozzone, A.; Grangeasse, C.
Staphylococcus aureus operates protein-tyrosine phosphorylation through a specific mechanism
J. Biol. Chem.
281
14048-14056
2006
Staphylococcus aureus (A8YPQ5), Staphylococcus aureus
brenda
Temel, D.B.; Dutta, K.; Alphonse, S.; Nourikyan, J.; Grangeasse, C.; Ghose, R.
Regulatory interactions between a bacterial tyrosine kinase and its cognate phosphatase
J. Biol. Chem.
288
15212-15228
2013
Escherichia coli (P76387), Escherichia coli
brenda
Wright, C.J.; Xue, P.; Hirano, T.; Liu, C.; Whitmore, S.E.; Hackett, M.; Lamont, R.J.
Characterization of a bacterial tyrosine kinase in Porphyromonas gingivalis involved in polymicrobial synergy
MicrobiologyOpen
3
383-394
2014
Porphyromonas gingivalis (B2RKZ8), Porphyromonas gingivalis, Porphyromonas gingivalis DSM 20709 (B2RKZ8)
brenda
Pereira, S.; Santos, M.; Leite, J.; Flores, C.; Eisfeld, C.; Buettel, Z.; Mota, R.; Rossi, F.; De Philippis, R.; Gales, L.; Morais-Cabral, J.; Tamagnini, P.
The role of the tyrosine kinase Wzc (Sll0923) and the phosphatase Wzb (Slr0328) in the production of extracellular polymeric substances (EPS) by Synechocystis PCC 6803
MicrobiologyOpen
8
e00753
2019
Synechocystis sp. PCC 6803 (P72877)
brenda
Olivares-Illana, V.; Meyer, P.; Bechet, E.; Gueguen-Chaignon, V.; Soulat, D.; Lazereg-Riquier, S.; Mijakovic, I.; Deutscher, J.; Cozzone, A.; Laprevote, O.; Morera, S.; Grangeasse, C.; Nessler, S.
Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus
PLoS Biol.
6
1321-1331
2008
Staphylococcus aureus (A8YPQ5), Staphylococcus aureus
brenda
Nourikyan, J.; Kjos, M.; Mercy, C.; Cluzel, C.; Morlot, C.; Noirot-Gros, M.F.; Guiral, S.; Lavergne, J.P.; Veening, J.W.; Grangeasse, C.
Autophosphorylation of the bacterial tyrosine-kinase CpsD connects capsule synthesis with the cell cycle in Streptococcus pneumoniae
PLoS Genet.
11
e1005518
2015
Streptococcus pneumoniae
brenda
Nakamoto, R.; Kwan, J.M.C.; Chin, J.F.L.; Ong, H.T.; Flores-Kim, J.; Midonet, C.; VanNieuwenhze, M.S.; Guan, X.L.; Sham, L.T.
The bacterial tyrosine kinase system CpsBCD governs the length of capsule polymers
Proc. Natl. Acad. Sci. USA
118
e2103377118
2021
Streptococcus pneumoniae
brenda
Wu, J.; Ohta, N.; Zhao, J.L.; Newton, A.
A novel bacterial tyrosine kinase essential for cell division and differentiation
Proc. Natl. Acad. Sci. USA
96
13068-13073
1999
Caulobacter vibrioides (Q9RQQ9), Caulobacter vibrioides, Caulobacter vibrioides ATCC 19089 (Q9RQQ9)
brenda
Hajredini, F.; Piserchio, A.; Ghose, R.
Long-range dynamic correlations regulate the catalytic activity of the bacterial tyrosine kinase Wzc
Sci. Adv.
6
eabd3718
2020
Escherichia coli (P76387), Escherichia coli
brenda
Hajredini, F.; Ghose, R.
An ATPase with a twist A unique mechanism underlies the activity of the bacterial tyrosine kinase, Wzc
Sci. Adv.
7
eabj5836
2021
Escherichia coli (P76387)
brenda
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