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ATP + H2O
ADP + phosphate
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
ATP + H2O + cholera toxin[side 1]
ADP + phosphate + cholera toxin[side 2]
ATP + H2O + WXG100 protein[side 1]
ADP + phosphate + WXG100 protein[side 2]
HopB1/in + ATP + H2O
HopB1/out + ADP + phosphate
-
intrinsic protein substrate, type II effector of pathogen
-
-
?
HopPtoN/in + ATP + H2O
HopPtoN/out + ADP + phosphate
-
Hrp outer protein effector of pathogen, that is translocated into host cells in enzyme-dependent secretion
-
-
?
HrpJ/in + ATP + H2O
HrpJ/out + ADP + phosphate
-
intrinsic protein substrate, its secretion is required for pathogenicity and translocation of effectors into plant cells
-
-
?
HrpK/in + ATP + H2O
HrpK/out + ADP + phosphate
-
intrinsic protein substrate, C-terminal half of protein is required for translocation
-
-
?
MgATP + H2O
MgADP + phosphate
-
-
-
-
?
YopR/in + ATP + H2O
YopR/out + ADP + phosphate
-
eleven N-terminal amino acids of YopR sectretion substrate function as secretion signal required for binding to enzyme
-
-
?
additional information
?
-
ATP + H2O
ADP + phosphate
-
secretion of amylase and protease
-
?
ATP + H2O
ADP + phosphate
-
a signature of the sec-dependent protein transport, by the type II and the type IV secretion, is the presence of a short, about 30 amino acids, mainly hydrophobic amino-terminal signal sequence in the exported protein. The signal sequence aids protein export and is cleaved off by a periplasmic signal peptidase when the exported protein reaches the periplasm
-
?
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
a signature of the sec-dependent protein transport, by the type II and the type IV secretion, is the presence of a short, about 30 amino acids, mainly hydrophobic amino-terminal signal sequence in the exported protein. The signal sequence aids protein export and is cleaved off by a periplasmic signal peptidase when the exported protein reaches the periplasm
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
type II protein secretion system exports flagellar subunits across the cytoplasmic membrane
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
the type III secretion system is dependent on ATPase activity, which catalyzes the unfolding of proteins and the secretion of effector proteins through the injectisome. CdsN, Cpn0707, is the T3S ATPase. CdsN interacts with CdsD, CdsL, CdsQ, and CopN, four putative structural components of the T3S system, CdsN also interacts with an unannotated protein, Cpn0706, a putative CdsN chaperone, overview
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
the type III secretion system is dependent on ATPase activity, which catalyzes the unfolding of proteins and the secretion of effector proteins through the injectisome. CdsN, Cpn0707, is the T3S ATPase. CdsN interacts with CdsD, CdsL, CdsQ, and CopN, four putative structural components of the T3S system, CdsN also interacts with an unannotated protein, Cpn0706, a putative CdsN chaperone, overview
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
secretion of pectate lyase and a cellulase through a type II secretion machinery, the Out system
-
?
ATP + H2O
ADP + phosphate
-
the cloned Erwinia chrysanthemi Hrp type III protein secretion system functions in Escherichia coli to deliver Pseudomonas syringae Avr signals to plant cells and to secrete Avr proteins in culture
-
?
ATP + H2O
ADP + phosphate
-
type II enzyme system: secretion of a large number of enzymes, including cellulases and pectinases
-
?
ATP + H2O
ADP + phosphate
-
in addition the protein binds DNA and interacts with PcfF and PcfG
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
?
ATP + H2O
ADP + phosphate
-
secretion of pectic enzymes and cellulase by the type II secretion system
-
?
ATP + H2O
ADP + phosphate
-
a signature of the sec-dependent protein transport, by the type II and the type IV secretion, is the presence of a short, about 30 amino acids, mainly hydrophobic amino-terminal signal sequence in the exported protein. The signal sequence aids protein export and is cleaved off by a periplasmic signal peptidase when the exported protein reaches the periplasm
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
?
ATP + H2O
ADP + phosphate
-
a signature of the sec-dependent protein transport, by the type II and the type IV secretion, is the presence of a short, about 30 amino acids, mainly hydrophobic amino-terminal signal sequence in the exported protein. The signal sequence aids protein export and is cleaved off by a periplasmic signal peptidase when the exported protein reaches the periplasm
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
PilB and PilT of the type IV pili, T4P, system in Myxococcus xanthus have ATPase activity acting at distinct steps in the T4P extension/retraction cycle in vivo
-
-
?
ATP + H2O
ADP + phosphate
-
PilB and PilT of the type IV pili, T4P, system in Myxococcus xanthus have ATPase activity in vitro
-
-
?
ATP + H2O
ADP + phosphate
-
PilB and PilT of the type IV pili, T4P, system in Myxococcus xanthus have ATPase activity acting at distinct steps in the T4P extension/retraction cycle in vivo
-
-
?
ATP + H2O
ADP + phosphate
-
PilB and PilT of the type IV pili, T4P, system in Myxococcus xanthus have ATPase activity in vitro
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
type II secretion apparatus is required for secretion of pectate lyase and cellulase
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system is required for secretion of pectinase and cellulase
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
type II enzyme: exports the largest number of proteins from this organism, including lipase, phospholipase C, alkaline phosphatase, exotoxin A, elastase and LasA. At least two different secretins are able to function in type II secretion: XcpQ and XqhA
-
?
ATP + H2O
ADP + phosphate
-
secretion of elastase, exotoxin A, phospholipase C, and other proteins
-
?
ATP + H2O
ADP + phosphate
-
a signature of the sec-dependent protein transport, by the type II and the type IV secretion, is the presence of a short, about 30 amino acids, mainly hydrophobic amino-terminal signal sequence in the exported protein. The signal sequence aids protein export and is cleaved off by a periplasmic signal peptidase when the exported protein reaches the periplasm
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
?
ATP + H2O
ADP + phosphate
-
the enzyme shows requirement for three invariant acidic residues in the Walker Asp Box motif, and for two invariant His residues in the His Box motif, structure-function analysis and modelling, overview. The Walker A motif is involved in ATP binding, while the Walker B motif is involved in the hydrolysis of ATP
-
-
?
ATP + H2O
ADP + phosphate
ATP binding structure with enzyme PscN, docking study
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
the enzyme shows requirement for three invariant acidic residues in the Walker Asp Box motif, and for two invariant His residues in the His Box motif, structure-function analysis and modelling, overview. The Walker A motif is involved in ATP binding, while the Walker B motif is involved in the hydrolysis of ATP
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
the Hrp type III protein secretion system catalyzes the Hrp pilus assembly
-
?
ATP + H2O
ADP + phosphate
-
plays a key role in secretion of the virulence proteins HrpW and AvrPto
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
secretion of the avirulence proteins HrmA and AvrPto from Pseudomonas syringae pathovars
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
FliH regulates the activity of the FliI ATPase and binds to FliI suppressing its oligomerization and ATPase activity. At the level of the export ATPase complex, two activities have been reported for FliJ, i.e. a T3SS chaperone escort activity and a stimulation of the FliI ATPase activity
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
FliI, an ATPase, provides the energy for export of the protein subunits, that form the filament and other structures to outside the membrane, via a specialized secretion apparatus, overview. This apparatus is related to the injectisome used by many gram-negative pathogens and symbionts to transfer effector proteins into host cells by type III secretion mechanism. Flagellar secretion in Salmonella enterica requires the proton motive force and does not require ATP hydrolysis by FliI. FliI is non-essential for flagellar assembly and function
-
-
?
ATP + H2O
ADP + phosphate
malachite green reagent assay for activity determination
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
malachite green reagent assay for activity determination
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
type III protein-secretion system delivers bacterial proteins into host cells that mediate this bacterium´s ability to enter nonpathogenic cells
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
the two type II secretion systems, SPI-1 and SPI-2 appear to play different roles during pathogenesis, with SPI-1 being required for initial penetration of the intestinal mucosa and SPI-2 necessary for subsequent systemic stages of infection
-
-
?
ATP + H2O
ADP + phosphate
-
FliI, the ATPase involved in bacterial flagellar protein export, forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
FliI, the ATPase involved in bacterial flagellar protein export, forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins
-
-
?
ATP + H2O
ADP + phosphate
-
type III protein-secretion system delivers bacterial proteins into host cells that mediate this bacterium´s ability to enter nonpathogenic cells
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
pathogens use the type III system as a key virulence mechanism
-
-
?
ATP + H2O
ADP + phosphate
-
invasion of epithelial cells by Shigella flexneri is mediated by a set of translocated bacterial invasins, the Ipa proteins, and its dedicated type III secretion system, Mxi-Spa
-
-
?
ATP + H2O
ADP + phosphate
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
secretion of AvrBs2 to pepper plants
-
?
ATP + H2O
ADP + phosphate
-
secretion of polygalacturonase
-
?
ATP + H2O
ADP + phosphate
-
a signature of the sec-dependent protein transport, by the type II and the type IV secretion, is the presence of a short, about 30 amino acids, mainly hydrophobic amino-terminal signal sequence in the exported protein. The signal sequence aids protein export and is cleaved off by a periplasmic signal peptidase when the exported protein reaches the periplasm
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
?
ATP + H2O
ADP + phosphate
-
The membrane-spanning type III secretion, T3S, system injects effector proteins into the cytosol of eukaryotic host cells, the T3S apparatus is associated with an ATPase that presumably provides the energy for the secretion process. HrcN is crucial for effector protein translocation and is essential for T3S and bacterial pathogenicity
-
-
?
ATP + H2O
ADP + phosphate
-
XpsE is the key component of the multi-protein complex of the type II secretion system T2SS, comprising 12 protein components, regulation occurs via Clp, a homologue of the cyclic AMP-receptor protein, by directly binding to the xpsE promoter region, overview
-
-
?
ATP + H2O
ADP + phosphate
-
HrcN hydrolyzes ATP in vitro
-
-
?
ATP + H2O
ADP + phosphate
-
XpsE possesses a nucleotide-binding Walker A motif involved in ATP binding
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
transport of AvrXa7
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
Yersinia enterolytica
-
-
-
?
ATP + H2O
ADP + phosphate
Yersinia enterolytica
-
-
-
?
ATP + H2O
ADP + phosphate
Yersinia enterolytica
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
the ATPase YscN is part of the type III secretion system, that translocates many virulence-related, bacterial effector proteins directly into the cytosol of host cells
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
pathogens use the type III system as a key virulence mechanism
-
-
?
ATP + H2O
ADP + phosphate
-
the type III secretion mechanism enables Yersinia sp. to inject a number of essential virulence determinants into the cytosol of host target cells. The injected proteins appear to interfere with host cell signal transduction pathway and other cellular processes, allowing Yersinia sp. to obstruct the primary immune response and to establish a systemic infaction
-
-
?
ATP + H2O
ADP + phosphate
-
YscU is an ATPase and a component of the Yersinia type III secretion machine, YscN is regulated by YscL, which binds YscU, an autocatalytically cleaving protease of the complex, YscN and YscU do not bind directly in vivo, interaction analysis, overview
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cholera toxin[side 1]
ADP + phosphate + cholera toxin[side 2]
-
-
-
?
ATP + H2O + cholera toxin[side 1]
ADP + phosphate + cholera toxin[side 2]
-
-
-
?
ATP + H2O + WXG100 protein[side 1]
ADP + phosphate + WXG100 protein[side 2]
-
-
-
-
?
ATP + H2O + WXG100 protein[side 1]
ADP + phosphate + WXG100 protein[side 2]
-
-
-
-
?
additional information
?
-
phosphate detection by malachite green assay
-
-
-
additional information
?
-
-
phosphate detection by malachite green assay
-
-
-
additional information
?
-
-
PilB and PilT are bipolar proteins belonging to the secretion NTPase superfamily, and power pilus extension and retraction, respectively, while the unipolar PilT paralogue PilU supports pilus retraction in an unknown manner. In all three proteins, the third acidic residue in the Asp Box and the second His of the His Box are crucial for function, mutation of these residues causes loss of PilT ATPase activity in vitro
-
-
?
additional information
?
-
phosphate detection by malachite green assay
-
-
-
additional information
?
-
phosphate detection by malachite green assay
-
-
-
additional information
?
-
-
phosphate detection by malachite green assay
-
-
-
additional information
?
-
-
PilB and PilT are bipolar proteins belonging to the secretion NTPase superfamily, and power pilus extension and retraction, respectively, while the unipolar PilT paralogue PilU supports pilus retraction in an unknown manner. In all three proteins, the third acidic residue in the Asp Box and the second His of the His Box are crucial for function, mutation of these residues causes loss of PilT ATPase activity in vitro
-
-
?
additional information
?
-
enzyme SsaN binds to Salmonella pathogenicity island 2 (SPI-2) specific chaperones, including SsaE, SseA, SscA, and SscB that facilitate translocator/effector secretion, SsaN dissociates a chaperone-effector complex, SsaE and SseB, in an ATP-dependent manner. Effector release is dependent on a conserved arginine residue at position 192 of SsaN, and this is essential for its enzymatic activity
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-
?
additional information
?
-
FliI is the ATPase energy donor of the flagellar type III export apparatus, interactions of flagellar chaperones with ATPase FliI, overview. FliT and the FliT-FliD complex bind to FliI
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-
?
additional information
?
-
T3SS ATPases functions as a docking site for chaperone-effector complexes, molecular mechanism by which SsaN captures these complexes to initiate translocation and recognizes the chaperones, overview. Modeling of the interaction between the multicargo chaperone, SrcA, and enzyme SsaN and validation of the model using SrcA mutagenesis to identify the residues on both the chaperone and ATPase that mediate the interaction
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?
additional information
?
-
-
T3SS ATPases functions as a docking site for chaperone-effector complexes, molecular mechanism by which SsaN captures these complexes to initiate translocation and recognizes the chaperones, overview. Modeling of the interaction between the multicargo chaperone, SrcA, and enzyme SsaN and validation of the model using SrcA mutagenesis to identify the residues on both the chaperone and ATPase that mediate the interaction
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-
?
additional information
?
-
enzyme SsaN binds to Salmonella pathogenicity island 2 (SPI-2) specific chaperones, including SsaE, SseA, SscA, and SscB that facilitate translocator/effector secretion, SsaN dissociates a chaperone-effector complex, SsaE and SseB, in an ATP-dependent manner. Effector release is dependent on a conserved arginine residue at position 192 of SsaN, and this is essential for its enzymatic activity
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-
?
additional information
?
-
-
MxiN interacts with and differentially regulates the activity of the enzyme in vivo
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-
?
additional information
?
-
-
radioactive 32P ATP substrate is hydrolyzed by the enzyme, producing either ADP and 32P (inorganic phosphate) or alpha-32P ADP and inorganic phosphate from gamma-32P ATP and alpha-32P ATP, respectively. Determination of enzyme kinetics of purified Spa47 using a direct alpha-32P ATPase assay. Though this method does not readily support real-time monitoring of product formation, it carries many inherent advantages including high signal-to-noise, capability with essentially any buffer conditions required to support enzyme stability, and no downstream coupling reactions required for product detection/quantitation, overview
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-
-
additional information
?
-
radioactive 32P ATP substrate is hydrolyzed by the enzyme, producing either ADP and 32P (inorganic phosphate) or alpha-32P ADP and inorganic phosphate from gamma-32P ATP and alpha-32P ATP, respectively. Determination of enzyme kinetics of purified Spa47 using a direct alpha-32P ATPase assay. Though this method does not readily support real-time monitoring of product formation, it carries many inherent advantages including high signal-to-noise, capability with essentially any buffer conditions required to support enzyme stability, and no downstream coupling reactions required for product detection/quantitation, overview
-
-
-
additional information
?
-
-
MxiN interacts with and differentially regulates the activity of the enzyme in vivo
-
-
?
additional information
?
-
basic assay developemnt for quantitatively measuring the in vitro activity of purified ATPases for functional characterization by detecting free phosphate through biding of malachite green molybdate, in vitro activity of the T2S ATPase EpsE can be stimulated by copurification of EpsE with the cytoplasmic domain of EpsL (EpsE-cytoEpsL) and addition of the acidic phospholipid cardiolipin. The assay consists of only one phosphate release measurement step, is highly sensitive, and can typically be performed within a few hours
-
-
-
additional information
?
-
basic assay developemnt for quantitatively measuring the in vitro activity of purified ATPases for functional characterization by detecting free phosphate through biding of malachite green molybdate, in vitro activity of the T2S ATPase EpsE can be stimulated by copurification of EpsE with the cytoplasmic domain of EpsL (EpsE-cytoEpsL) and addition of the acidic phospholipid cardiolipin. The assay consists of only one phosphate release measurement step, is highly sensitive, and can typically be performed within a few hours
-
-
-
additional information
?
-
basic assay developemnt for quantitatively measuring the in vitro activity of purified ATPases for functional characterization by detecting free phosphate through biding of malachite green molybdate, in vitro activity of the T2S ATPase EpsE can be stimulated by copurification of EpsE with the cytoplasmic domain of EpsL (EpsE-cytoEpsL) and addition of the acidic phospholipid cardiolipin. The assay consists of only one phosphate release measurement step, is highly sensitive, and can typically be performed within a few hours
-
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-
additional information
?
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-
stability of HrcN depends on the conserved HrcL protein, which interacts with HrcN in vitro and in vivo, overexpression of HrcL affects bacterial pathogenicity. HrcN also interacts with the T3S substrate specificity switch protein HpaC and the global T3S chaperone HpaB, which promotes secretion of multiple effector proteins, protein-protein interaction studies, overview
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?
additional information
?
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HrcN dissociates a complex between HpaB and the effector protein XopF1 in an ATP-dependent manner. The effector release depends on a conserved glycine residue in the HrcN phosphate-binding loop, which is crucial for enzymatic activity and protein function during membrane-spanning type III secretion, T3S
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?
additional information
?
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enzyme ATPase HrcN interacts with its regulator HrcL and substrate acceptor site HrcQ
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?
additional information
?
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enzyme ATPase HrcN interacts with its regulator HrcL and substrate acceptor site HrcQ
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?
additional information
?
-
-
YscN does not bind to the fused chaperone SycE with effector YopE, overview
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?
additional information
?
-
phosphate detection by malachite green assay
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-
additional information
?
-
phosphate detection by malachite green assay
-
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-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O
ADP + phosphate
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
ATP + H2O + cholera toxin[side 1]
ADP + phosphate + cholera toxin[side 2]
HopB1/in + ATP + H2O
HopB1/out + ADP + phosphate
-
intrinsic protein substrate, type II effector of pathogen
-
-
?
HopPtoN/in + ATP + H2O
HopPtoN/out + ADP + phosphate
-
Hrp outer protein effector of pathogen, that is translocated into host cells in enzyme-dependent secretion
-
-
?
HrpJ/in + ATP + H2O
HrpJ/out + ADP + phosphate
-
intrinsic protein substrate, its secretion is required for pathogenicity and translocation of effectors into plant cells
-
-
?
HrpK/in + ATP + H2O
HrpK/out + ADP + phosphate
-
intrinsic protein substrate, C-terminal half of protein is required for translocation
-
-
?
additional information
?
-
ATP + H2O
ADP + phosphate
-
secretion of amylase and protease
-
-
?
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
the type III secretion system is dependent on ATPase activity, which catalyzes the unfolding of proteins and the secretion of effector proteins through the injectisome. CdsN, Cpn0707, is the T3S ATPase. CdsN interacts with CdsD, CdsL, CdsQ, and CopN, four putative structural components of the T3S system, CdsN also interacts with an unannotated protein, Cpn0706, a putative CdsN chaperone, overview
-
-
?
ATP + H2O
ADP + phosphate
-
the type III secretion system is dependent on ATPase activity, which catalyzes the unfolding of proteins and the secretion of effector proteins through the injectisome. CdsN, Cpn0707, is the T3S ATPase. CdsN interacts with CdsD, CdsL, CdsQ, and CopN, four putative structural components of the T3S system, CdsN also interacts with an unannotated protein, Cpn0706, a putative CdsN chaperone, overview
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
the cloned Erwinia chrysanthemi Hrp type III protein secretion system functions in Escherichia coli to deliver Pseudomonas syringae Avr signals to plant cells and to secrete Avr proteins in culture
-
?
ATP + H2O
ADP + phosphate
-
type II enzyme system: secretion of a large number of enzymes, including cellulases and pectinases
-
?
ATP + H2O
ADP + phosphate
-
in addition the protein binds DNA and interacts with PcfF and PcfG
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
?
ATP + H2O
ADP + phosphate
-
secretion of pectic enzymes and cellulase by the type II secretion system
-
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
?
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
PilB and PilT of the type IV pili, T4P, system in Myxococcus xanthus have ATPase activity acting at distinct steps in the T4P extension/retraction cycle in vivo
-
-
?
ATP + H2O
ADP + phosphate
-
PilB and PilT of the type IV pili, T4P, system in Myxococcus xanthus have ATPase activity acting at distinct steps in the T4P extension/retraction cycle in vivo
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system is required for secretion of pectinase and cellulase
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
secretion of elastase, exotoxin A, phospholipase C, and other proteins
-
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
?
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
the Hrp type III protein secretion system catalyzes the Hrp pilus assembly
-
-
?
ATP + H2O
ADP + phosphate
-
secretion of the avirulence proteins HrmA and AvrPto from Pseudomonas syringae pathovars
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
?
ATP + H2O
ADP + phosphate
-
FliH regulates the activity of the FliI ATPase and binds to FliI suppressing its oligomerization and ATPase activity. At the level of the export ATPase complex, two activities have been reported for FliJ, i.e. a T3SS chaperone escort activity and a stimulation of the FliI ATPase activity
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
FliI, an ATPase, provides the energy for export of the protein subunits, that form the filament and other structures to outside the membrane, via a specialized secretion apparatus, overview. This apparatus is related to the injectisome used by many gram-negative pathogens and symbionts to transfer effector proteins into host cells by type III secretion mechanism. Flagellar secretion in Salmonella enterica requires the proton motive force and does not require ATP hydrolysis by FliI. FliI is non-essential for flagellar assembly and function
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-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
type III protein-secretion system delivers bacterial proteins into host cells that mediate this bacterium´s ability to enter nonpathogenic cells
-
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
?
ATP + H2O
ADP + phosphate
-
the two type II secretion systems, SPI-1 and SPI-2 appear to play different roles during pathogenesis, with SPI-1 being required for initial penetration of the intestinal mucosa and SPI-2 necessary for subsequent systemic stages of infection
-
-
?
ATP + H2O
ADP + phosphate
-
FliI, the ATPase involved in bacterial flagellar protein export, forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins
-
-
?
ATP + H2O
ADP + phosphate
-
FliI, the ATPase involved in bacterial flagellar protein export, forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins
-
-
?
ATP + H2O
ADP + phosphate
-
type III protein-secretion system delivers bacterial proteins into host cells that mediate this bacterium´s ability to enter nonpathogenic cells
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
?
ATP + H2O
ADP + phosphate
-
pathogens use the type III system as a key virulence mechanism
-
-
?
ATP + H2O
ADP + phosphate
-
invasion of epithelial cells by Shigella flexneri is mediated by a set of translocated bacterial invasins, the Ipa proteins, and its dedicated type III secretion system, Mxi-Spa
-
-
?
ATP + H2O
ADP + phosphate
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
secretion of AvrBs2 to pepper plants
-
-
?
ATP + H2O
ADP + phosphate
-
secretion of polygalacturonase
-
-
?
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
?
ATP + H2O
ADP + phosphate
-
The membrane-spanning type III secretion, T3S, system injects effector proteins into the cytosol of eukaryotic host cells, the T3S apparatus is associated with an ATPase that presumably provides the energy for the secretion process. HrcN is crucial for effector protein translocation and is essential for T3S and bacterial pathogenicity
-
-
?
ATP + H2O
ADP + phosphate
-
XpsE is the key component of the multi-protein complex of the type II secretion system T2SS, comprising 12 protein components, regulation occurs via Clp, a homologue of the cyclic AMP-receptor protein, by directly binding to the xpsE promoter region, overview
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-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
Yersinia enterolytica
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
the ATPase YscN is part of the type III secretion system, that translocates many virulence-related, bacterial effector proteins directly into the cytosol of host cells
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
?
ATP + H2O
ADP + phosphate
-
pathogens use the type III system as a key virulence mechanism
-
-
?
ATP + H2O
ADP + phosphate
-
the type III secretion mechanism enables Yersinia sp. to inject a number of essential virulence determinants into the cytosol of host target cells. The injected proteins appear to interfere with host cell signal transduction pathway and other cellular processes, allowing Yersinia sp. to obstruct the primary immune response and to establish a systemic infaction
-
-
?
ATP + H2O
ADP + phosphate
-
YscU is an ATPase and a component of the Yersinia type III secretion machine, YscN is regulated by YscL, which binds YscU, an autocatalytically cleaving protease of the complex, YscN and YscU do not bind directly in vivo, interaction analysis, overview
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
-
?
ATP + H2O + cholera toxin[side 1]
ADP + phosphate + cholera toxin[side 2]
-
-
-
?
ATP + H2O + cholera toxin[side 1]
ADP + phosphate + cholera toxin[side 2]
-
-
-
?
additional information
?
-
-
PilB and PilT are bipolar proteins belonging to the secretion NTPase superfamily, and power pilus extension and retraction, respectively, while the unipolar PilT paralogue PilU supports pilus retraction in an unknown manner. In all three proteins, the third acidic residue in the Asp Box and the second His of the His Box are crucial for function, mutation of these residues causes loss of PilT ATPase activity in vitro
-
-
?
additional information
?
-
-
PilB and PilT are bipolar proteins belonging to the secretion NTPase superfamily, and power pilus extension and retraction, respectively, while the unipolar PilT paralogue PilU supports pilus retraction in an unknown manner. In all three proteins, the third acidic residue in the Asp Box and the second His of the His Box are crucial for function, mutation of these residues causes loss of PilT ATPase activity in vitro
-
-
?
additional information
?
-
enzyme SsaN binds to Salmonella pathogenicity island 2 (SPI-2) specific chaperones, including SsaE, SseA, SscA, and SscB that facilitate translocator/effector secretion, SsaN dissociates a chaperone-effector complex, SsaE and SseB, in an ATP-dependent manner. Effector release is dependent on a conserved arginine residue at position 192 of SsaN, and this is essential for its enzymatic activity
-
-
?
additional information
?
-
FliI is the ATPase energy donor of the flagellar type III export apparatus, interactions of flagellar chaperones with ATPase FliI, overview. FliT and the FliT-FliD complex bind to FliI
-
-
?
additional information
?
-
T3SS ATPases functions as a docking site for chaperone-effector complexes, molecular mechanism by which SsaN captures these complexes to initiate translocation and recognizes the chaperones, overview. Modeling of the interaction between the multicargo chaperone, SrcA, and enzyme SsaN and validation of the model using SrcA mutagenesis to identify the residues on both the chaperone and ATPase that mediate the interaction
-
-
?
additional information
?
-
-
T3SS ATPases functions as a docking site for chaperone-effector complexes, molecular mechanism by which SsaN captures these complexes to initiate translocation and recognizes the chaperones, overview. Modeling of the interaction between the multicargo chaperone, SrcA, and enzyme SsaN and validation of the model using SrcA mutagenesis to identify the residues on both the chaperone and ATPase that mediate the interaction
-
-
?
additional information
?
-
enzyme SsaN binds to Salmonella pathogenicity island 2 (SPI-2) specific chaperones, including SsaE, SseA, SscA, and SscB that facilitate translocator/effector secretion, SsaN dissociates a chaperone-effector complex, SsaE and SseB, in an ATP-dependent manner. Effector release is dependent on a conserved arginine residue at position 192 of SsaN, and this is essential for its enzymatic activity
-
-
?
additional information
?
-
-
stability of HrcN depends on the conserved HrcL protein, which interacts with HrcN in vitro and in vivo, overexpression of HrcL affects bacterial pathogenicity. HrcN also interacts with the T3S substrate specificity switch protein HpaC and the global T3S chaperone HpaB, which promotes secretion of multiple effector proteins, protein-protein interaction studies, overview
-
-
?
additional information
?
-
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enzyme ATPase HrcN interacts with its regulator HrcL and substrate acceptor site HrcQ
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additional information
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enzyme ATPase HrcN interacts with its regulator HrcL and substrate acceptor site HrcQ
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evolution
enzyme FliI is a member of the Walker-type ATPase family
evolution
phylogenetic analysis and tree of T3SS ATPases, overview
evolution
the enzyme contains a two-helix-finger motif at the entrance of the modeled central pore of the InvC hexamer. The motif is highly conserved among type III secretion-associated ATPases, including those associated with the flagellar assembly apparatus. In addition to the tyrosine residue (Tyr385 in InvC) located at the center of the loop, other residues within the loop are highly conserved, such as Gly383, Glu384, and Gly388. Similarities between type III secretion ATPases and other ATP-driven protein translocases/unfoldases
evolution
the T2SS secretion ATPase GspE belongs to the family of Type II/IV secretion ATPases
evolution
VirB11 belongs to the superfamily of traffic ATPases, which includes members of the type II secretion system and the type IV pilus and archaeal flagellar assembly apparatus
evolution
ATPase DotB belongs to the VirB11 family of proteins, but sequence analysis reveals that DotB might be more related to PilT/EpsE family proteins than VirB11 family proteins. The subunits DotBL from Legionella pneumophila and DotBY from Yersinia pseudotuberculosis display a very similar topology
evolution
ATPase DotB belongs to the VirB11 family of proteins, but sequence analysis reveals that DotB might be more related to PilT/EpsE family proteins than VirB11 family proteins. The subunits DotBL from Legionella pneumophila and DotBY from Yersinia pseudotuberculosis display a very similar topology. The N-terminal domain of DotBL adopts a PAS-like fold, similar to PilT, EpsE, and HP0525
evolution
EpsE is a AAA+ ATPase and member of the bacterial Type II/IV secretion subfamily of NTPases
evolution
-
ATPase DotB belongs to the VirB11 family of proteins, but sequence analysis reveals that DotB might be more related to PilT/EpsE family proteins than VirB11 family proteins. The subunits DotBL from Legionella pneumophila and DotBY from Yersinia pseudotuberculosis display a very similar topology
-
evolution
-
VirB11 belongs to the superfamily of traffic ATPases, which includes members of the type II secretion system and the type IV pilus and archaeal flagellar assembly apparatus
-
evolution
-
EpsE is a AAA+ ATPase and member of the bacterial Type II/IV secretion subfamily of NTPases
-
evolution
-
the enzyme contains a two-helix-finger motif at the entrance of the modeled central pore of the InvC hexamer. The motif is highly conserved among type III secretion-associated ATPases, including those associated with the flagellar assembly apparatus. In addition to the tyrosine residue (Tyr385 in InvC) located at the center of the loop, other residues within the loop are highly conserved, such as Gly383, Glu384, and Gly388. Similarities between type III secretion ATPases and other ATP-driven protein translocases/unfoldases
-
evolution
-
EpsE is a AAA+ ATPase and member of the bacterial Type II/IV secretion subfamily of NTPases
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malfunction
-
abrogation of the interaction between the CesABEspA complex and EscN resulted in severe secretion and infection defects
malfunction
loss of enzyme BsaS function either via direct genetic inactivation or treatment with the inhibitor compound 939 results in increased susceptibility of Burkholderia pseudomallei to microtubule-associated protein light chain 3-associated phagocytosis in infected RAW 264.7 cells, leading to elevated levels of intracellular killing. The bsaS deletion mutant is highly attenuated for virulence in BALB/c mice
malfunction
secretion of glyceraldehyde-3-phosphate dehydrogenase is abolished in mutants defective in the type III ATPase EscN. Complementation with escN gene restores GAPDH secretion
malfunction
complementing a spa47 null Shigella flexneri strain with the inactive Spa47K165A mutant results in the same lack of invasiveness seen for the null strain. The hemolysis results presented suggest that Shigella strains lacking the gene for Spa47 or strains complemented with ATPase inactive Spa47 mutants are not able to properly insert the translocon into the host membrane. This seems to be a direct result of an inability of the mutant strains to secrete IpaB and IpaC and properly deliver them to the host cell membrane. Phenotype, overview
malfunction
-
loss of enzyme BsaS function either via direct genetic inactivation or treatment with the inhibitor compound 939 results in increased susceptibility of Burkholderia pseudomallei to microtubule-associated protein light chain 3-associated phagocytosis in infected RAW 264.7 cells, leading to elevated levels of intracellular killing. The bsaS deletion mutant is highly attenuated for virulence in BALB/c mice
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metabolism
enteropathogenic (EPEC) Escherichia coli secrete GAPDH through a type III secretion system into the culture medium. GAPDH secretion is not linked to outer membrane vesicles and depends on growth conditions. The secretion process is often dependent on a bacterial chaperone. The chaperone CesT displays broad substrate specificity and plays a central role in the recruitment of multiple type III effectors to the T3SS apparatus
metabolism
Gram-negative bacteria use the type II secretion (T2S) system to secrete exoproteins for attacking animal or plant cells or to obtain nutrients from the environment. The system is unique in helping folded proteins traverse the outer membrane. The secretion machine comprises multiple proteins spanning the cell envelope and a cytoplasmic ATPase. Activity of the ATPase, when copurified with the cytoplasmic domain of an interactive ATPase partner, is stimulated by an acidic phospholipid, suggesting the membrane-associated ATPase is actively engaged in secretion
metabolism
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pathogenicity of many Gram-negative bacteria depends on a type III secretion (T3S) system which translocates bacterial effector proteins into eukaryotic cells. The membrane-spanning secretion apparatus is associated with a cytoplasmic ATPase complex and a predicted cytoplasmic (C) ring structure which is proposed to provide a substrate docking platform for secreted proteins. The putative C ring component HrcQ from the plant pathogenic bacterium Xanthomonas campestris pv. vesicatoria is essential for bacterial pathogenicity and type III secretion system, overview. The general substrate acceptor site of the T3S system, HrcQ, localizes to the cytoplasm and associates with the bacterial membranes under type III secretion system-permissive conditions binding to the cytoplasmic T3S-ATPase HrcN, its predicted regulator HrcL and the cytoplasmic domains of the inner membrane proteins HrcV and HrcU. HpaB presumably targets effector proteins to the ATPase HrcN of the T3S system which can dissociate HpaB-effector protein complexes and thus might facilitate the entry of effector proteins into the inner channel of the T3S system
metabolism
the enzyme is an ATPase enzyme involved in the type III secretion system, T3SS
metabolism
the enzyme is part of the type II secretion system (T2SS), which is present in many Gram-negative bacteria and is responsible for secreting a large number of folded proteins, including major virulence factors, across the outer membrane
metabolism
the type II secretion system (T2SS), a multiprotein machinery spanning two membranes in Gram-negative bacteria, incudes the critical multidomain GspEEpsE, and is responsible for the secretion of folded proteins from the periplasm across the outer membrane
metabolism
type III secretion system T3SS-1 facilitates host cell invasion and inflammation, whereas type III secretion system T3SS-2 mediates intracellular survival and immune evasion
metabolism
type III secretion systems (T3SS) are a primary mechanism employed by Chlamydia to interact with the eukaryotic host cell, enabling access to the intracellular environment, modification of the early endosome and to establish and maintain an intracellular environment. T3SSs are a critical component of two bacterial systems: the flagellum, an extracellular motor essential to motility,4,5 and the non-flagellar (NF)-T3SS, an energy-dependent, molecular syringe that facilitates the transport of host-altering effector proteins into the host cytosol during infection
metabolism
Shigella rely entirely on the actions of a complex T3SS to inject effector proteins into the cytoplasm of host cells, initiating cellular invasion of the colonic epithelium and onset of infection. The Shigella T3SS consists of about 54 genes that reside on a 220-kb virulence plasmid. The entry region of the virulence plasmid contains the mxi, spa, and ipa operons that code for the type III secretion apparatus (T3SA) itself. T3SS ATPases have been identified in several T3SSs
metabolism
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type III secretion systems (T3SS) are a primary mechanism employed by Chlamydia to interact with the eukaryotic host cell, enabling access to the intracellular environment, modification of the early endosome and to establish and maintain an intracellular environment. T3SSs are a critical component of two bacterial systems: the flagellum, an extracellular motor essential to motility,4,5 and the non-flagellar (NF)-T3SS, an energy-dependent, molecular syringe that facilitates the transport of host-altering effector proteins into the host cytosol during infection
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metabolism
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pathogenicity of many Gram-negative bacteria depends on a type III secretion (T3S) system which translocates bacterial effector proteins into eukaryotic cells. The membrane-spanning secretion apparatus is associated with a cytoplasmic ATPase complex and a predicted cytoplasmic (C) ring structure which is proposed to provide a substrate docking platform for secreted proteins. The putative C ring component HrcQ from the plant pathogenic bacterium Xanthomonas campestris pv. vesicatoria is essential for bacterial pathogenicity and type III secretion system, overview. The general substrate acceptor site of the T3S system, HrcQ, localizes to the cytoplasm and associates with the bacterial membranes under type III secretion system-permissive conditions binding to the cytoplasmic T3S-ATPase HrcN, its predicted regulator HrcL and the cytoplasmic domains of the inner membrane proteins HrcV and HrcU. HpaB presumably targets effector proteins to the ATPase HrcN of the T3S system which can dissociate HpaB-effector protein complexes and thus might facilitate the entry of effector proteins into the inner channel of the T3S system
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metabolism
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type III secretion system T3SS-1 facilitates host cell invasion and inflammation, whereas type III secretion system T3SS-2 mediates intracellular survival and immune evasion
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physiological function
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deletion of the catalytic domain of the yscN gene in Yersinia pestis CO92 attenuated the strain over three million-fold in the Swiss-Webster mouse model of bubonic plague
physiological function
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interaction of ATPase InvC with type III secretion effector SopD. SopD helix II region, residues 268-302, is essential for the interaction with InvC
physiological function
the N-terminal domain of ATPase FliI interacts with the cytoplasmic domain of falgellar ortholog FlhA, but not with FliF. The FlhA binding domain resides in the N-terminal 150 amino acids of FliI. FliI also interacts with flagellar proteins CdsL and CopN
physiological function
a two-helix-finger motif and a conserved loop located at the entrance of and within the predicted pore formed by the hexameric ATPase are essential for the ATP-driven protein translocase InvC function in the type III secretion system. Type III secretion machines are essential for the virulence or symbiotic relationships of many bacteria. An essential component of these machines is a highly conserved ATPase, which is necessary for the recognition and secretion of proteins destined to be delivered by the type III secretion pathway, e.g. secretion of the regulatory protein InvJ (early substrate), the translocases SipB, SipC, and SipD (middle substrate), and the effector proteins SptP and SopB (late substrates)
physiological function
among the many protein components of the T2SS, the secretion ATPase GspE plays an essential role, and is likely responsible for providing energy for the protein translocation process
physiological function
enzyme SsaN hydrolyzes ATP in vitro and is essential for type III secretion system, T3SS, function and Salmonella virulence in vivo. Protein-protein interaction analyses reveal that SsaN interacts with SsaK and SsaQ to form the C ring complex. The T3SS-2-associated ATPase SsaN contributes to T3SS-2 effector translocation efficiency. Enzyme SsaN is required for the export of another T3SS-2 effector, SseJ, which is encoded outside of the T3SS-2 region. Enzyme SsaN releases the translocator protein SseB from the T3SS-2 specific chaperone SsaE in an ATP-dependent manner. Gene ssaN contributes to Salmonella virulence in the mouse model of systemic infection
physiological function
Gram-negative pathogens utilize type III secretion systems (T3SSs) to inject bacterial effector proteins into the host. An important component of T3SSs is a conserved ATPase that captures chaperone-effector complexes and energizes their dissociation to facilitate effector translocation. Chaperones engage type III secretion system ATPases to facilitate effector secretion, molecular basis of the chaperone-T3SS ATPase interaction interface, modeling of the interaction between the multicargo chaperone, SrcA, and the enzyme SsaN, overview. Importance of the chaperone-T3SS ATPase interaction for the pathogenesis of Salmonella
physiological function
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HrcQ interacts with conserved components of the type-III secretion system at the inner membrane including the inner membrane proteins HrcV and HrcU, the ATPase HrcN and its predicted regulator HrcL
physiological function
proper recognition, unfolding, and secretion of substrates in both type III secretion systems are regulated by interactions between the T3SS ATPase and ATPase-regulator proteins, presence of both flagellar and NF-T3SS ATPase/ATPase-regulator pairs in Chlamydia
physiological function
proper recognition, unfolding, and secretion of substrates in both type III secretion systems are regulated by interactions between the T3SS ATPase and ATPase-regulator proteins, presence of both flagellar and NF-T3SS ATPase/ATPase-regulator pairs in Chlamydia, interactions between the flagellar ATPase (FliI) and the NF-T3SS ATPase regulator (CdsL)
physiological function
the enzyme ATPase foci colocalizes with the secretion channel. The ATPase may be transiently associated with the T2S machine by alternating between a cytoplasmic and a machine-associated state in a secretion-dependent manner, terminating the ATPase activity when secretion is completed. Function-related dynamic assembly may be the essence of the T2S machine, overview. The T2S ATPase acts as a transiently associated part of the secretion machine
physiological function
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the enzyme is the key protein in the type III secretion (TTS) system, a multi-protein machinery that has evolved to deliver bacterial virulence proteins directly into eukaryotic cells, through an organelle termed the injectisome. The ATPase EscN is a peripheral membrane protein located at the entrance of the injectisome, at the cytoplasmic base of the injectisome, and forms a ring structure. Enzyme EscN selectively engages the EspA-loaded CesAB, but not the unliganded CesAB. The targeting signal is encoded in a disorder-order structural transition in CesAB that is elicited only upon binding of its physiological substrate, EspA. There is no interaction between CesAB and EscN, CesAB appears not to be engaged by the injectisome ATPase in its substrate-free form, but the CesABEspA heterodimer interacts specifically with the EscN ATPase mediated by CesAB. Efficient targeting of CesAB-EspA to ATPase EscN is required for EspA secretion
physiological function
the enzyme YsaN is negatively regulated by YsaL, overview
physiological function
the flagellar type III export apparatus consists of a proton-driven export gate and an ATPase complex. The export process is well regulated by dynamic, specific and cooperative interactions among export components, chaperones, and export substrates in a timely manner
physiological function
the flagellar type III export apparatus consists of a proton-driven export gate and an ATPase complex. The export process is well regulated by dynamic, specific and cooperative interactions among export components, chaperones, and export substrates in a timely manner. Chaperone FliD binds to FliI and significantly enhances or stabilizes the weak interaction between the C-terminal ATPase domain FliICAT and flagellar chaperone FliT94 presumably through cooperative interactions among FliICAT, FliD and FliT94. Because FliH suppresses ATP hydrolysis by FliI, FliH coordinates ATP hydrolysis by FliI with protein export
physiological function
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ATP hydrolysis by the enzyme alone can drive flagellar protein export without proton motive force
physiological function
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enzyme form vT3SS is involved in virulence
physiological function
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enzyme form vT3SS is involved in virulence while enzyme form fT3SS uis essential for flagellar assembly and cell motility
physiological function
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the enzyme is involved in the motility and pathogenicity of avian pathogenic Escherichia coli and contributes to bacterial colonization and virulence during systemic infection in vivo
physiological function
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the enzyme is necessary for cellular invasion . The enzyme provides the energy for the type three secretion apparatus which penetrates the host cell membrane and provides a unidirectional conduit for injection of effectors into host cells
physiological function
adenosine triphosphate-hydrolyzing enzymes, or ATPases, play a critical role in a diverse array of cellular functions. These dynamic proteins can generate energy for mechanical work, such as protein trafficking and degradation, solute transport, and cellular movements. EpsE powers type II secretion (T2S) in Vibrio cholerae, the causative agent of cholera. The T2S system is responsible for the secretion of a wide variety of proteins
physiological function
functional analysis of type three secretion system ATPase PscN and its regulator PscL from Pseudomonas aeruginosa, PscL inhibits PscN ATPase activity up to 80% when mixed with PscN in 1:2 ratio (PscN:PscL)
physiological function
Legionella pneumophila utilizes a type IVb secretion (T4bS) system termed dot/icm to secrete protein effectors to the host cytoplasm. The dot/icm system is powered at least in part by a functionally critical AAA1 ATPase, a protein called DotB
physiological function
Shigella virulence is entirely reliant on ATPase active Spa47 and its activity is driven by oligomerization. Type III secretion system ATPase activation and Shigella virulence regulation mechanism by enzyme Spa47, mutational analysis, overview. ATPase inactive full-length Spa47 point mutants show, that Spa47 oligomerization and ATP hydrolysis are needed for complete T3SS apparatus formation, a proper translocator secretion profile, and Shigella virulence, structure-function analysis. Active Spa47 is required for proper T3SS translocon formation and Shigella flexneri host cell invasion. ATPase activity is an essential factor in Shigella virulence. Shigella T3SS translocator secretion requires T3SS ATPase activity
physiological function
the Shigella protein Spa47 is an ATPase that supports protein secretion through its specialized type three secretion apparatus (T3SA), supporting infection of human host cells
physiological function
the type IVb secretion (T4bS) system termed dot/icm secretes protein effectors to the host cytoplasm. The dot/icm system is powered at least in part by a functionally critical AAA1 ATPase, a protein called DotB
physiological function
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the type IVb secretion (T4bS) system termed dot/icm secretes protein effectors to the host cytoplasm. The dot/icm system is powered at least in part by a functionally critical AAA1 ATPase, a protein called DotB
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physiological function
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the enzyme is involved in the motility and pathogenicity of avian pathogenic Escherichia coli and contributes to bacterial colonization and virulence during systemic infection in vivo
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physiological function
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adenosine triphosphate-hydrolyzing enzymes, or ATPases, play a critical role in a diverse array of cellular functions. These dynamic proteins can generate energy for mechanical work, such as protein trafficking and degradation, solute transport, and cellular movements. EpsE powers type II secretion (T2S) in Vibrio cholerae, the causative agent of cholera. The T2S system is responsible for the secretion of a wide variety of proteins
-
physiological function
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proper recognition, unfolding, and secretion of substrates in both type III secretion systems are regulated by interactions between the T3SS ATPase and ATPase-regulator proteins, presence of both flagellar and NF-T3SS ATPase/ATPase-regulator pairs in Chlamydia
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physiological function
-
proper recognition, unfolding, and secretion of substrates in both type III secretion systems are regulated by interactions between the T3SS ATPase and ATPase-regulator proteins, presence of both flagellar and NF-T3SS ATPase/ATPase-regulator pairs in Chlamydia, interactions between the flagellar ATPase (FliI) and the NF-T3SS ATPase regulator (CdsL)
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physiological function
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HrcQ interacts with conserved components of the type-III secretion system at the inner membrane including the inner membrane proteins HrcV and HrcU, the ATPase HrcN and its predicted regulator HrcL
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physiological function
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enzyme SsaN hydrolyzes ATP in vitro and is essential for type III secretion system, T3SS, function and Salmonella virulence in vivo. Protein-protein interaction analyses reveal that SsaN interacts with SsaK and SsaQ to form the C ring complex. The T3SS-2-associated ATPase SsaN contributes to T3SS-2 effector translocation efficiency. Enzyme SsaN is required for the export of another T3SS-2 effector, SseJ, which is encoded outside of the T3SS-2 region. Enzyme SsaN releases the translocator protein SseB from the T3SS-2 specific chaperone SsaE in an ATP-dependent manner. Gene ssaN contributes to Salmonella virulence in the mouse model of systemic infection
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physiological function
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a two-helix-finger motif and a conserved loop located at the entrance of and within the predicted pore formed by the hexameric ATPase are essential for the ATP-driven protein translocase InvC function in the type III secretion system. Type III secretion machines are essential for the virulence or symbiotic relationships of many bacteria. An essential component of these machines is a highly conserved ATPase, which is necessary for the recognition and secretion of proteins destined to be delivered by the type III secretion pathway, e.g. secretion of the regulatory protein InvJ (early substrate), the translocases SipB, SipC, and SipD (middle substrate), and the effector proteins SptP and SopB (late substrates)
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physiological function
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adenosine triphosphate-hydrolyzing enzymes, or ATPases, play a critical role in a diverse array of cellular functions. These dynamic proteins can generate energy for mechanical work, such as protein trafficking and degradation, solute transport, and cellular movements. EpsE powers type II secretion (T2S) in Vibrio cholerae, the causative agent of cholera. The T2S system is responsible for the secretion of a wide variety of proteins
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physiological function
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the enzyme is necessary for cellular invasion . The enzyme provides the energy for the type three secretion apparatus which penetrates the host cell membrane and provides a unidirectional conduit for injection of effectors into host cells
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additional information
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a recombinant well folded CesAB D14L/R18D/E20L mutant homodimer variant binds specifically to EscN in contrast to the monomeric form
additional information
enzyme structure molecular modeling, overview
additional information
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enzyme structure molecular modeling, overview
additional information
flagellar type III export apparatus structure analysis, structure-function relationship, overview. Because FliI binds to FlhAC and the C-terminal domain of FlhB (FlhBC), the FliI6-FliJ ring complex is formed on the FlhAC-FlhBC platform and is stably anchored to the platform through the interaction between FliHEN and FlhATM
additional information
flagellar type III export apparatus structure analysis, structure-function relationship, overview. Because FliI binds to FlhAC and the C-terminal domain of FlhB (FlhBC), the FliI6-FliJ ring complex is formed on the FlhAC-FlhBC platform and is stably anchored to the platform through the interaction between FliHEN and FlhATM
additional information
molecular docking studies and protein-protein interaction network of pscN ATPase, overview
additional information
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molecular docking studies and protein-protein interaction network of pscN ATPase, overview
additional information
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protein-protein interactions involving CT398, RpoN, and both flagellar and non-flagellar T3SS ATPase and ATPase regulators, overview. CT398 functions as a regulatory protein partner in several key areas of chlamydial biology, including as a posttranslational chaperone of RpoN and as a modulator of T3S-dependent events, CT398 protein structure analysis, detailed overview
additional information
protein-protein interactions involving CT398, RpoN, and both flagellar and non-flagellar T3SS ATPase and ATPase regulators, overview. CT398 functions as a regulatory protein partner in several key areas of chlamydial biology, including as a posttranslational chaperone of RpoN and as a modulator of T3S-dependent events, CT398 protein structure analysis, detailed overview
additional information
structure-function relationship, modeling based on the crystal structures of EscN, a T3SS ATPase from enteropathogenic Escherichia coli, PDB IDs 2OBM and 2OBL, and a crystal structure of the F1 ATPase hexamer, PDB ID 1BMF, overview. K165 is the catalytic residue of the ATPase
additional information
the conserved arginine residue at position 192 of SsaN located in the dicyclohexylcarbodiimide-binding site (DCCD box) in the catalytic domain is essential for ATPase activity
additional information
enzyme residues K417 and K419 do not contribute to EpsE's basal activity but rather to the ability of the protein to be stimulated by cardiolipin
additional information
enzyme structure determination, analysis, and comparison, overview
additional information
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enzyme structure determination, analysis, and comparison, overview
additional information
enzyme structure determination, analysis, and comparison, overview
additional information
in oligomeric Spa47, ATP hydrolysis may be supported by specific side chain contributions from adjacent protomers within the complex, structure analysis and modelling of an activated oligomeric Spa47, overview. ATPase inactive full-length Spa47 point mutants show, that Spa47 oligomerization and ATP hydrolysis are needed for complete T3SS apparatus formation, a proper translocator secretion profile, and Shigella virulence. Regulation of Spa47 oligomerization in vivo. Key catalytic residues are spatially conserved in Spa47. Generation of an activated hexameric Spa47 model. The predicted active site residues are Lys165 and Glu188, as well as Arg350
additional information
in oligomeric Spa47, ATP hydrolysis may be supported by specific side chain contributions from adjacent protomers within the complex, structure analysis and modelling of an activated oligomeric Spa47, overview. ATPase inactive full-length Spa47 point mutants show, that Spa47 oligomerization and ATP hydrolysis are needed for complete T3SS apparatus formation, a proper translocator secretion profile, and Shigella virulence. Regulation of Spa47 oligomerization in vivo. Key catalytic residues are spatially conserved in Spa47. Generation of an activated hexameric Spa47 model. The predicted active site residues are Lys165 and Glu188, as well as Arg350
additional information
PscN possesses G-X-X-P and G-X-P sequence motifs (X-any amino acid) in its primary sequences which are frequently found in the peptide channels and putative membrane ion channels. These motifs can be attributed to the N-terminal flexibility of the protein
additional information
PscN possesses G-X-X-P and G-X-P sequence motifs (X-any amino acid) in its primary sequences which are frequently found in the peptide channels and putative membrane ion channels. These motifs can be attributed to the N-terminal flexibility of the protein
additional information
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PscN possesses G-X-X-P and G-X-P sequence motifs (X-any amino acid) in its primary sequences which are frequently found in the peptide channels and putative membrane ion channels. These motifs can be attributed to the N-terminal flexibility of the protein
additional information
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enzyme structure determination, analysis, and comparison, overview
-
additional information
-
enzyme residues K417 and K419 do not contribute to EpsE's basal activity but rather to the ability of the protein to be stimulated by cardiolipin
-
additional information
-
protein-protein interactions involving CT398, RpoN, and both flagellar and non-flagellar T3SS ATPase and ATPase regulators, overview. CT398 functions as a regulatory protein partner in several key areas of chlamydial biology, including as a posttranslational chaperone of RpoN and as a modulator of T3S-dependent events, CT398 protein structure analysis, detailed overview
-
additional information
-
the conserved arginine residue at position 192 of SsaN located in the dicyclohexylcarbodiimide-binding site (DCCD box) in the catalytic domain is essential for ATPase activity
-
additional information
-
structure-function relationship, modeling based on the crystal structures of EscN, a T3SS ATPase from enteropathogenic Escherichia coli, PDB IDs 2OBM and 2OBL, and a crystal structure of the F1 ATPase hexamer, PDB ID 1BMF, overview. K165 is the catalytic residue of the ATPase
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additional information
-
enzyme residues K417 and K419 do not contribute to EpsE's basal activity but rather to the ability of the protein to be stimulated by cardiolipin
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x * 47500, calculated
?
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component EscC, 54000, component EscV, 72000, component EscN, 49000
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x * 70000, GST-tagged enzyme, SDS-PAGE
?
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x * 55520, calculated from amino acid sequence
?
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x * 50000, SDS-PAGE
-
?
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x * 50000, SDS-PAGE
-
?
-
x * 64000, YscN, SDS-PAGE
dodecamer
12 * 48000, SDS-PAGE, predominant form at membrane, activity increases 700fold over monomeric form
dodecamer
-
cryo-electron microscopy
dodecamer
12 * 49500, recombinant His-tagged enzyme, SDS-PAGE. The enzyme exists in solution as higher order oligomer. The ATPase activity of oligomeric YsaN is several fold higher than the activity of the monomeric form
hexamer
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hexamer
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full-length EscN forms a stable hexamer in solution with stimulated ATPase activity
hexamer
6 * 169000, recombinant full-length enzyme, SDS-PAGE
hexamer
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6 * 169000, recombinant full-length enzyme, SDS-PAGE
-
hexamer
-
nucleotide binding locks enzyme hexamer into a symmetric and compact structure, in absence of nucleotide, the N-terminal domain exhibits a collection of rigid-body conformations, crystallization data and analytical ultracentrifugation
hexamer
6 * 44000, SDS-PAGE, DotBL forms an asymmetric hexamer, subunit interaction analysis, three intersubunit interfaces, protein-protein interfaces between subunits, detailed overview
hexamer
PscN exists predominantly as oligomer
hexamer
6 * 48000, SDS-PAGE
hexamer
-
6 * 48000, SDS-PAGE
hexamer
-
FliI forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins
hexamer
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FliI forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins
-
hexamer
structure overview
hexamer
6 * 38900, calculated from amino acid sequence
hexamer
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6 * 38900, calculated from amino acid sequence
-
hexamer
-
6 * 100000, SDS-PAGE
homohexamer
fully active enzyme form, FliI forms hetero-trimers along with the FliH dimer
homohexamer
6 * 44000, SDS-PAGE
homohexamer
6 * 48000, SDS-PAGE
homohexamer
-
secretion NTPases of the type II secretion and type IV pili systems, including PilB, PilT and PilU, function as toroidal homohexamers and, in addition toWalker A and Walker B motifs, contain unique Asp Box and His Box motifs
homohexamer
6 * 47900, calculated from amino acid sequence
homohexamer
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secretion NTPases of the type II secretion and type IV pili systems, including PilB, PilT and PilU, function as toroidal homohexamers and, in addition toWalker A and Walker B motifs, contain unique Asp Box and His Box motifs
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homohexamer
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6 * 48000, SDS-PAGE
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homohexamer
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6 * 47900, calculated from amino acid sequence
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homohexamer
a two-helix-finger motif and a conserved loop located at the entrance of and within the predicted pore formed by the hexameric ATPase, structure modeling
homohexamer
fully active enzyme form
homohexamer
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a two-helix-finger motif and a conserved loop located at the entrance of and within the predicted pore formed by the hexameric ATPase, structure modeling
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monomer
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1 * 62000, recombinant His-tagged PilB, SDS-PAGE, x * 63800, about, His6-tagged PilB, sequence calculation, 1 * 39000, recombinant His-tagged PilT, SDS-PAGE, 1 * 41000, about, His6-tagged PilT, sequence calculation
monomer
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1 * 62000, recombinant His-tagged PilB, SDS-PAGE, x * 63800, about, His6-tagged PilB, sequence calculation, 1 * 39000, recombinant His-tagged PilT, SDS-PAGE, 1 * 41000, about, His6-tagged PilT, sequence calculation
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monomer
1 * 48000, SDS-PAGE
monomer
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1 * 48000, SDS-PAGE
oligomer
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x * 48100, about, sequence calculation, SDS-PAGE, CdsN forms oligomers and high-molecular-weight multimers, possibly dodecamers
oligomer
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x * 48100, about, sequence calculation, SDS-PAGE, CdsN forms oligomers and high-molecular-weight multimers, possibly dodecamers
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oligomer
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different oligomeric forms are identified by blue native electrophoresis, including a hexamer and a dodecamer
trimer
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3 * 48000, SDS-PAGE
trimer
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3 * 48000, SDS-PAGE
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trimer
3 * 83000, GspE-cyto-GspL complex, crystal structure analysis
additional information
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enzyme associates with intrinsic protein exeB to forms large complexes
additional information
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fliI encodes a 50000 Da polypeptide ATPase, fliJ encodes a 16000 Da hydrophobic protein of unknown function
additional information
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the outer-membrane lipoprotein OutS interacts directly with the C-terminal end of the secretin OutD
additional information
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the Out proteins form a membrane-associated multiprotein complex, OutE is the putative ATP binding component and OutL is an inner membrane protein. OutE and OutL interact directly. OutE induces a conformational change in OutL, in both its cytoplasmic and periplasmic domains. The secretion process requires a conformational change in OutE which depends on both the interaction with OutL and on the presence of an intact Walker A motif in OutE
additional information
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the secretory pathway comprises a number of inner membrane proteins, SecD to SecF, SecY, a cytoplasmic membrane-associated ATPase, SecA, that provides the energy for export, a chaperone, SecB, that binds to presecretory target proteins, and the periplasmic signal peptidase
additional information
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effector Tir is not required for chaperone and enzyme interactions, enzyme binds effector specifically without its chaperone
additional information
the DotBL subunit is composed of an about 150 amino acids long N-terminal domain (NTD), comprising 6 beta-strands and 3 alpha-helices, and an about 250 amino acids C-terminal domain (CTD) consisting of 7 beta-strands and 10 alpha-helices. The two domains are connected by a 10 amino acids proline-rich linker
additional information
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the DotBL subunit is composed of an about 150 amino acids long N-terminal domain (NTD), comprising 6 beta-strands and 3 alpha-helices, and an about 250 amino acids C-terminal domain (CTD) consisting of 7 beta-strands and 10 alpha-helices. The two domains are connected by a 10 amino acids proline-rich linker
additional information
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PilB and PilT proteins do not form oligomers under all conditions tested, overview
additional information
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PilB and PilT proteins do not form oligomers under all conditions tested, overview
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additional information
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Out C, OutD, OutE and OutF are proteins of the Put apparatus, OutC is a cytoplasmic membrane protein with a single transmembrane domain and a large hydrophilic periplasmic domain, OutF is a cytoplasmic membrane protein with three transmembrane domains, a small periplasmic loop, a large cytoplasmic loop and an N-terminal cytoplasmic domain
additional information
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-
additional information
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the general secretion pathway requires the participation of 12 proteins, of which XcpT, XcpU, XcpV, XcpW are homologues of PilA, the major subunit of type IV pili. PilA itself is necessary for optimal secretion of proteins demonstrating that the pathway of type IV pilus assembly and the operation of the apparatus of the general secretion pathway are overlapping processes
additional information
the PscN primary structure shows three different domains: N-terminal (residues 1-95), central ATPase (residues 96-370), and C-terminal domain (residues 370-440), PscN tertiary structure analysis, overview
additional information
the PscN primary structure shows three different domains: N-terminal (residues 1-95), central ATPase (residues 96-370), and C-terminal domain (residues 370-440), PscN tertiary structure analysis, overview
additional information
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the PscN primary structure shows three different domains: N-terminal (residues 1-95), central ATPase (residues 96-370), and C-terminal domain (residues 370-440), PscN tertiary structure analysis, overview
additional information
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-
additional information
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several components of the type III secretion system are organized in a supramolecular structure termed needle complex. This structure is made of discrete structures including a base that spans both membranes and a needle-like projection that extends outwards from the bacterial surface. The type III secretion export apparatus is required for the assembly of the needle substructure but is dispensable for the assembly of the base. The length of the needle segment is determined by the type III secretion associated protein InvJ. InvG, PrgH, and PrgK constitute the base. PrgI is the main component of the needle of the type III secretion complex. The needle component may establish the specificity of type III secretion system in delivering proteins into either plant or animal cells
additional information
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model of domain construction and complex of subunits
additional information
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structure analysis and comparison using crystal structure PDB code DPY
additional information
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structure analysis and comparison using crystal structure PDB code DPY
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additional information
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several components of the type III secretion system are organized in a supramolecular structure termed needle complex. This structure is made of discrete structures including a base that spans both membranes and a needle-like projection that extends outwards from the bacterial surface. The type III secretion export apparatus is required for the assembly of the needle substructure but is dispensable for the assembly of the base. The length of the needle segment is determined by the type III secretion associated protein InvJ. InvG, PrgH, and PrgK constitute the base. PrgI is the main component of the needle of the type III secretion complex. The needle component may establish the specificity of type III secretion system in delivering proteins into either plant or animal cells
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additional information
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-
additional information
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the lipidated protein MxiM is required in type III secretion
additional information
analysis of Spa47 oligomeric distribution
additional information
analysis of Spa47 oligomeric distribution
additional information
recombinant enzyme GspE-Hcp1 fusion proteins, i.e. DELTAN1GspEEpsE-KLASGHcp1, DELTAN1GspEEpsE-GSGSGS-Hcp1, DELTAN1GspEEpsE-KLASGAGHcp1, and DELTAN1GspEEpsE-KLASGAGH-Hcp1, show homogeneous hexamer formation, structure analysis, detailed overview. The hexamerization enhances the ATPase activity of these four DN1GspEEpsE-linker-Hcp1 variants compared to monomeric DN1GspEEpsE by more than 20fold. The metal binding domains are located on the periphery of both DN1GspEEpsE hexamers
additional information
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recombinant enzyme GspE-Hcp1 fusion proteins, i.e. DELTAN1GspEEpsE-KLASGHcp1, DELTAN1GspEEpsE-GSGSGS-Hcp1, DELTAN1GspEEpsE-KLASGAGHcp1, and DELTAN1GspEEpsE-KLASGAGH-Hcp1, show homogeneous hexamer formation, structure analysis, detailed overview. The hexamerization enhances the ATPase activity of these four DN1GspEEpsE-linker-Hcp1 variants compared to monomeric DN1GspEEpsE by more than 20fold. The metal binding domains are located on the periphery of both DN1GspEEpsE hexamers
additional information
GspE is a protein of about 500 residues folding into three major domains, the N-terminal domains N1E and N2E, and the C-terminal domain CTE. The N2E and CTE domains of a single GspE subunit adopt a mutual orientation
additional information
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GspE is a protein of about 500 residues folding into three major domains, the N-terminal domains N1E and N2E, and the C-terminal domain CTE. The N2E and CTE domains of a single GspE subunit adopt a mutual orientation
additional information
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analysis of protein-protein interactions of type III secretion system, ATPase HrcN has a hexameric ring structure
additional information
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additional information
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association of the cytoplasmic membrane protein XpsN, MW 36000 Da determined by SDS-PAGE, with the outer membrane protein XpsD in the type II protein secretion apparatus
additional information
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XpsE possesses a nucleotide-binding Walker A motif
additional information
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upon addition of ATP, purified enzyme forms aggregates, probably hexamers
additional information
the DotBY subunit is composed of an about 150 amino acids long N-terminal domain (NTD), comprising 6 beta-strands and 3 alpha-helices, and an about 250 amino acids C-terminal domain (CTD) consisting of 7 beta-strands and 10 alpha-helices. The two domains are connected by a 10 aminoacids proline-rich linker
additional information
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the DotBY subunit is composed of an about 150 amino acids long N-terminal domain (NTD), comprising 6 beta-strands and 3 alpha-helices, and an about 250 amino acids C-terminal domain (CTD) consisting of 7 beta-strands and 10 alpha-helices. The two domains are connected by a 10 aminoacids proline-rich linker
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deltaN103
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pcfF mutant lacking codon 1 to 103
EscNDELTA102
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EscN mutant
EscNDELTA102-V393P
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mutant, used for crystallization
EscNDELTA7-R366D
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EscN mutant
R113E
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no ATPase activity
R133E
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dramatic decrease in ATPase activity
R18A
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dramatic decrease in hexameric particles, increase ATPase activity
C110R
naturally occurring mutation, a class I mutant, has hexamerization defects, and is located at the NTDn/CTDn11 interface
D35N
naturally occurring mutation, a class IV mutant, has hexamerization defects, and is located at the NTDn/CTDn11 interface
G234D
naturally occurring mutation, a class IV mutant
H253R
naturally occurring mutation, a class IV mutant
K162N/Q
naturally occurring mutation, a class I mutant
K182E
naturally occurring mutation, a class I mutant, has hexamerization defects, and is located at the NTDn/CTDn11 interface
L111P
naturally occurring mutation, a class I mutant, has hexamerization defects, and is located at the NTDn/CTDn11 interface
N180I
naturally occurring mutation, a class IV mutant, has hexamerization defects, and is located at the NTDn/CTDn11 interface
R270C
naturally occurring mutation, the mutant is partially functional and can harbor a loss of function due a conformation-switch defect, since Arg270 is part of the critical lower CTDn/CTDn11 interface
S163L
naturally occurring mutation, a class I mutant
E205A
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a Walker B box substitution in PilT, leads to strong reduction of ATPase activity due to direct interference with ATP hydrolysis
E391A
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a Walker B box substitution in PilB, leads to strong reduction of ATPase activity due to direct interference with ATP hydrolysis
K137A
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a Walker A box substitution in PilT, leads to abolishment of ATPase activity due to indirect interference withe ATP binding
K327A
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a Walker A box substitution in PilB, leads to strong reduction of ATPase activity due to indirect interference withe ATP binding
E205A
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a Walker B box substitution in PilT, leads to strong reduction of ATPase activity due to direct interference with ATP hydrolysis
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E391A
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a Walker B box substitution in PilB, leads to strong reduction of ATPase activity due to direct interference with ATP hydrolysis
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K137A
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a Walker A box substitution in PilT, leads to abolishment of ATPase activity due to indirect interference withe ATP binding
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K327A
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a Walker A box substitution in PilB, leads to strong reduction of ATPase activity due to indirect interference withe ATP binding
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D160N
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mutation in the Walker A motif of PilT, and in PilU
E159Q
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mutation in the Walker A motif of PilT, and in PilU
E163Q
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mutation in the Walker A motif of PilT, and in PilU
E204
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mutation in the Walker B motif of PilT, and in PilU, inactive PilT mutant
G135S
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mutation in the Asp Box of PilT, and in PilU, inactive PilT mutant
H222A
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mutation in the His Box of PilT, and in PilU
H229A
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mutation in the His Box of PilT, and in PilU
E16A
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the mutation slightly reduces the binding affinity of the ATPase FliI for FliH
E383A
site-directed mutagenesis, the mutant shows almost unaltered protein secretion activity compared to the wild-type
E384A
site-directed mutagenesis, the mutant shows reduced protein secretion activity compared to the wild-type
E384A/Y385A
site-directed mutagenesis, the mutant shows reduced protein secretion activity compared to the wild-type
E384A/Y385A/G388A
site-directed mutagenesis, the mutant shows markedly reduced protein secretion activity and reduced ATPase activity compared to the wild-type
F15A
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the mutation slightly reduces the binding affinity of the ATPase FliI for FliH
G164C
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loss-of-function mutant, unable to hydrolyze ATP, decrease in ability to interact with themselves and wild-type enzyme molecules
G388A
site-directed mutagenesis, the mutant shows slightly reduced protein secretion activity compared to the wild-type
K165E
site-directed mutagenesis, InvC ATPase inactive enzyme mutant
L12A
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the mutation significantly reduces the binding affinity of the ATPase FliI for FliH
L376P
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loss-of-function mutant, defective in type II secretion and infection of cultured cells, wild-type ATP-ase activity
R189G
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loss-of-function mutant, unable to hydrolyze ATP
R191H
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loss-of-function mutant, unable to hydrolyze ATP, decrease in ability to interact with themselves and wild-type enzyme molecules
R192G
site-directed mutagenesis of the conserved arginine residue at position 192 of SsaN located in the dicyclohexylcarbodiimide-binding site in the catalytic domain, inactive mutant showing no ATPase and translocation activity. Introducing a plasmid that expresses SsaNR192G into the DELTAssaN mutant fails to complement SseJ secretion. Mutant SsaNR192G-Myc-His6 binds to chaperone SsaE
R223H
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loss-of-function mutant, unable to hydrolyze ATP
R26A/R27A/R33A
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the mutations significantly reduce the binding affinity of the ATPase FliI for FliH
R4A
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the mutation significantly reduces the binding affinity of the ATPase FliI for FliH
R4A/R7A
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the mutation significantly reduces the binding affinity of the ATPase FliI for FliH
R7A
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the mutation slightly reduces the binding affinity of the ATPase FliI for FliH
V28M
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loss-of-function mutant, defective in type II secretion and infection of cultured cells, wild-type ATP-ase activity
V51E
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loss-of-function mutant, defective in type II secretion and infection of cultured cells, wild-type ATP-ase activity
W8A
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the mutation significantly reduces the binding affinity of the ATPase FliI for FliH
Y385A
site-directed mutagenesis, the Salmonelly typhimurium mutant strain expressing InvCY385A shows a marked defect in its ability to secrete the effector proteins SptP and SopB, while expression of the substrate proteins is unaffected by introduction of mutations in InvC, the mutant shows reduced ATPase activity compared to the wild-type
Y385W
site-directed mutagenesis, the mutant shows reduced ATPase activity compared to the wild-type
E383A
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site-directed mutagenesis, the mutant shows almost unaltered protein secretion activity compared to the wild-type
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E384A
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site-directed mutagenesis, the mutant shows reduced protein secretion activity compared to the wild-type
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K165E
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site-directed mutagenesis, InvC ATPase inactive enzyme mutant
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R192G
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site-directed mutagenesis of the conserved arginine residue at position 192 of SsaN located in the dicyclohexylcarbodiimide-binding site in the catalytic domain, inactive mutant showing no ATPase and translocation activity. Introducing a plasmid that expresses SsaNR192G into the DELTAssaN mutant fails to complement SseJ secretion. Mutant SsaNR192G-Myc-His6 binds to chaperone SsaE
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Y385A
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site-directed mutagenesis, the Salmonelly typhimurium mutant strain expressing InvCY385A shows a marked defect in its ability to secrete the effector proteins SptP and SopB, while expression of the substrate proteins is unaffected by introduction of mutations in InvC, the mutant shows reduced ATPase activity compared to the wild-type
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Y385W
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site-directed mutagenesis, the mutant shows reduced ATPase activity compared to the wild-type
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E211Q
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the mutant enzyme can bind Mg2-ATP to form a hexameric ring and associate with the export gate but has no ATP hydrolyzing activity
E718A
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catalytic site mutant which is unaffected in ATP binding
K654A
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the Walker A motif site mutant shows about 90% less ATP binding compared to the wild type enzyme
C400S
the mutant is almost inactive
C430S
the mutant is almost inactive
C430S/C433S
the mutant is almost inactive
C400S
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the mutant is almost inactive
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C430S
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the mutant is almost inactive
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C430S/C433S
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the mutant is almost inactive
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G175C
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catalytically inactive mutant
R286A
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XpsE mutant hydrolysis ATP at a rate five times that of the wild-type XpsE, but is non-functional in protein secretion via T2SS
K175E
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mutation in one of hte Walker boxes, enzymatically inactive
R104E
inactive
R104E
naturally occurring mutation, a class IV mutant, located at the NTDn/CTDn11 interface
R123E
inactive
R123E
naturally occurring mutation, a class IV mutant, located at the NTDn/CTDn11 interface
E188A
inactive
E188A
site-directed mutagenesis, ATPase-inactive active site mutant, the mutation has little effect on the global structure of the protein
K165A
-
inactive
K165A
site-directed mutagenesis, ATPase-inactive active site mutant, the mutation has little effect on the global structure of the protein
R350A
inactive
R350A
site-directed mutagenesis, ATPase-inactive active site mutant, the mutation has little effect on the global structure of the protein
K417A/K419A
site-directed mutagenesis, the double lysine mutation in the EpsE zinc-binding domain highly reduces stimulated ATPase activity compared to wild-type by reducing the stimulation through cardiolipin
K417A/K419A
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site-directed mutagenesis, the double lysine mutation in the EpsE zinc-binding domain highly reduces stimulated ATPase activity compared to wild-type by reducing the stimulation through cardiolipin
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K417A/K419A
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site-directed mutagenesis, the double lysine mutation in the EpsE zinc-binding domain highly reduces stimulated ATPase activity compared to wild-type by reducing the stimulation through cardiolipin
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additional information
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expression of N-terminal cytoplasmic domain, domain shows ATPase activity
additional information
generation of a bsaS deletion mutant, the bsaS deletion mutant is highly attenuated for virulence in BALB/c mice
additional information
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generation of a bsaS deletion mutant, the bsaS deletion mutant is highly attenuated for virulence in BALB/c mice
additional information
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generation of a bsaS deletion mutant, the bsaS deletion mutant is highly attenuated for virulence in BALB/c mice
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additional information
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the GST-tagged C-terminal truncation mutant of CdsN possesses ATPase activity
additional information
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the GST-tagged C-terminal truncation mutant of CdsN possesses ATPase activity
-
additional information
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escV nonpolar deletion mutant, accumulation of EscC in periplasm. escN nonpolar deletion mutant, accumulation of EscC in periplasm
additional information
gene disruption mutant, shows reduced secretion of pilD-dependent enzymatic activities, mutants are greatly impaired for growth within Hartmannella vermiformis. Upon infection of U937 macrophages, mutant strains exhibit a 10fold reduction in intracellular multiplication and a diminished cytopathic effect
additional information
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gene disruption mutant, shows reduced secretion of pilD-dependent enzymatic activities, mutants are greatly impaired for growth within Hartmannella vermiformis. Upon infection of U937 macrophages, mutant strains exhibit a 10fold reduction in intracellular multiplication and a diminished cytopathic effect
additional information
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construction of diverse Walker A and Walker B boxe mutants, PilB as well as PilT ATPase activity is abolished in vitro by replacement of conserved residues in the Walker A and Walker B boxes that are involved in ATP binding and hydrolysis, respectively, cell phenotypes, overview
additional information
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construction of diverse Walker A and Walker B boxe mutants, PilB as well as PilT ATPase activity is abolished in vitro by replacement of conserved residues in the Walker A and Walker B boxes that are involved in ATP binding and hydrolysis, respectively, cell phenotypes, overview
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additional information
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a spa47 mutant is constructed by inserting a kanamycin-resistance gene into the spa47 gene, spa47 encodes a putative ATPase, the mutant HI4320spa47omegakan displays no growth defect
additional information
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a constructed YFP-PilB construct does not complement a pilB mutant, mutation of conserved Walker A or Walker B residues in any of PilB, PilT and PilU ATPases abrogates twitching motility, and for the Walker A mutant of PilT causes loss of polar localization, overview
additional information
crosslinking of the ATPase-regulator complex with 2% glutaraldehyde at 27°C for 5 min in 20 mM phosphate, pH 8.0, and 100 mM NaCl, PscN-PscL structure modelling, overview
additional information
crosslinking of the ATPase-regulator complex with 2% glutaraldehyde at 27°C for 5 min in 20 mM phosphate, pH 8.0, and 100 mM NaCl, PscN-PscL structure modelling, overview
additional information
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crosslinking of the ATPase-regulator complex with 2% glutaraldehyde at 27°C for 5 min in 20 mM phosphate, pH 8.0, and 100 mM NaCl, PscN-PscL structure modelling, overview
additional information
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weak swarming motility and rare flagella are observed in a mutant deleted for FliI and for the nonflagellar type III secretion ATPases InvJ and SsaN
additional information
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deletion mutants of regulatory protein FliH, deletion of last five residues causes 5fold activation of ATPase activity, FliH N-terminus stabilizes complex with ATPase subunit, residues between 99 and 235 required for interaction with ATPase
additional information
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generation of in-frame 10-residue deletion mutations within the 100 residues of the N-terminal domain. The oligomerization and FliH-binding ability are retained and the ATPase activity is maintained in most of the deletion variants, except for DELTA6 mutant and partially for DELTA1 mutant, DELTA4 mutant shows inhibited motility compared to the wild-type enzyme, mutant DELTA2 and DELTA4, as well as DELTA35-38 show 1.3, 5.7, and 2fold increased ATPase activity, overview
additional information
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generation of in-frame 10-residue deletion mutations within the 100 residues of the N-terminal domain. The oligomerization and FliH-binding ability are retained and the ATPase activity is maintained in most of the deletion variants, except for DELTA6 mutant and partially for DELTA1 mutant, DELTA4 mutant shows inhibited motility compared to the wild-type enzyme, mutant DELTA2 and DELTA4, as well as DELTA35-38 show 1.3, 5.7, and 2fold increased ATPase activity, overview
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additional information
N-terminal domain truncation results in strictly monomeric enzyme that is unable to hydrolyze ATP, despite maintaining the canonical ATPase core structure and active site residues
additional information
N-terminal domain truncation results in strictly monomeric enzyme that is unable to hydrolyze ATP, despite maintaining the canonical ATPase core structure and active site residues
additional information
although N-terminal domain truncation is necessary for crystal formation, it results in strictly monomeric Spa47 that is unable to hydrolyze ATP, despite maintaining the canonical ATPase core structure and active site residues. ATPase inactive full-length Spa47 point mutants show, that Spa47 oligomerization and ATP hydrolysis are needed for complete T3SS apparatus formation, a proper translocator secretion profile, and Shigella virulence. Generation of an activated hexameric Spa47 model. Construction and expression of diverse ATPase-inactive Spa47 mutants in Shigella, phenotypes, overview. The truncated mutant Spa47DELTA1-79 is ATPase-inactive
additional information
although N-terminal domain truncation is necessary for crystal formation, it results in strictly monomeric Spa47 that is unable to hydrolyze ATP, despite maintaining the canonical ATPase core structure and active site residues. ATPase inactive full-length Spa47 point mutants show, that Spa47 oligomerization and ATP hydrolysis are needed for complete T3SS apparatus formation, a proper translocator secretion profile, and Shigella virulence. Generation of an activated hexameric Spa47 model. Construction and expression of diverse ATPase-inactive Spa47 mutants in Shigella, phenotypes, overview. The truncated mutant Spa47DELTA1-79 is ATPase-inactive
additional information
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N-terminal domain truncation results in strictly monomeric enzyme that is unable to hydrolyze ATP, despite maintaining the canonical ATPase core structure and active site residues
-
additional information
four hexamers of Vibrio cholerae GspEEpsE are obtained when fused to Hcp1 as an assistant hexamer, shown with native mass spectrometry. The enzymatic activity of the GspEEpsE-Hcp1 fusions is about 20 times higher than that of a GspEEpsE monomer. Crystal structures of GspEEpsE-Hcp1 fusions with different linker lengths reveal regular and elongated hexamers of GspEEpsE with major differences in domain orientation within subunits, and in subunit assembly
additional information
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four hexamers of Vibrio cholerae GspEEpsE are obtained when fused to Hcp1 as an assistant hexamer, shown with native mass spectrometry. The enzymatic activity of the GspEEpsE-Hcp1 fusions is about 20 times higher than that of a GspEEpsE monomer. Crystal structures of GspEEpsE-Hcp1 fusions with different linker lengths reveal regular and elongated hexamers of GspEEpsE with major differences in domain orientation within subunits, and in subunit assembly
additional information
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construction of a hrcN deletion mutant
additional information
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overexpression of the clp gene in Xcc wild-type strain 8004 enhances the production of XpsE as well as endoglucanase and extracellular polysaccharide. Deactivation of the clp gene by Tn5 transposon insertion at the coding sequence of the clp gene, resulting in mutant XC472, reduces XpsE expression levels, overview
additional information
fluorescent-tagged ATPase expressed in secretion-proficient cells is mainly diffused in cytoplasm. Focal spots at the cell periphery are detectable only in a few cells. The discrete foci are augmented in abundance and intensity when the secretion channel is depleted and the exoprotein overproduced, overview. The foci abundance is inversely related to secretion efficiency of the secretion channel. Restored function of the secretion channel paralleles reduced ATPase foci abundance
additional information
-
fluorescent-tagged ATPase expressed in secretion-proficient cells is mainly diffused in cytoplasm. Focal spots at the cell periphery are detectable only in a few cells. The discrete foci are augmented in abundance and intensity when the secretion channel is depleted and the exoprotein overproduced, overview. The foci abundance is inversely related to secretion efficiency of the secretion channel. Restored function of the secretion channel paralleles reduced ATPase foci abundance
additional information
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GST fusions of the cytoplasmic T3S ATPase HrcN and its predicted regulator HrcL are immobilized on glutathione sepharose and incubated with a bacterial lysate containing HrcQ-c-Myc, binding and interaction analysis, overview
additional information
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GST fusions of the cytoplasmic T3S ATPase HrcN and its predicted regulator HrcL are immobilized on glutathione sepharose and incubated with a bacterial lysate containing HrcQ-c-Myc, binding and interaction analysis, overview
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additional information
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fusion of YscP with glutathione S-transferase leads to blockage of type III secretion and formation of type III secretion needles requiring the YscP secretion signal sequence, mutational analysis of sequences required for the blockage, overview
additional information
generation of several truncation mutants of YsaN for identification of critical residues of YsaN for stable YsaL-YsaN complex formation, overview. Crosslinking of purified His-tagged enzyme YsaN and His-tagged regulator YsaL, pH 8.0, 25°C, using 0.5 mM ethylene glycol bis(sulfosuccinimidylsuccinate) and 1.5% glutaraldehyde, respectively
additional information
-
generation of several truncation mutants of YsaN for identification of critical residues of YsaN for stable YsaL-YsaN complex formation, overview. Crosslinking of purified His-tagged enzyme YsaN and His-tagged regulator YsaL, pH 8.0, 25°C, using 0.5 mM ethylene glycol bis(sulfosuccinimidylsuccinate) and 1.5% glutaraldehyde, respectively
additional information
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three different strains expressing simultaneously a short and a long version of YscP are engineered (Short YscP protein,YscP388: the spacer between the two export signals and one copy of the repeats in the central part are removed. Long YscP, yscP686: a restriction cleavage site between codons 250 and 251 in the central part of the yscP gene is engineered. A copy of codons 214-374, encoding the repeated region, into the restriction site is inserted). Genetic evidence is provided that only one molecule of YscP is required to control the length of one injectisome needle, thus supporting the static model of needle length regulation
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Martinez, A.; Ostrovsky, P.; Nunn, D.N.
Identification of an additional member of the secretin superfamily of proteins in Pseudomonas aeruginosa that is able to function in type II protein secretion
Mol. Microbiol.
28
1235-1246
1998
Pseudomonas aeruginosa
brenda
Lu, H.M.; Motley, S.T.; Lory, S.
Interactions of the components of the general secretion pathway: role of Pseudomonas aeruginosa type IV pilin subunits in complex formation and extracellular protein secretion
Mol. Microbiol.
25
247-259
1997
Pseudomonas aeruginosa
brenda
Shevchik, V.E.; Condemine, G.
Functional characterization of the Erwinia chrysanthemi OutS protein, an element of a type II secretion system
Microbiology
144
3219-3228
1998
Dickeya chrysanthemi
brenda
Ham, J.H.; Bauer, D.W.; Fouts, D.E.; Collmer, A.
A cloned Erwinia chrysanthemi Hrp (type III protein secretion) system functions in Escherichia coli to deliver Pseudomonas syringae Avr signals to plant cells and to secrete Avr proteins in culture
Proc. Natl. Acad. Sci. USA
95
10206-10211
1998
Dickeya chrysanthemi
brenda
Py, B.; Loiseau, L.; Barras, F.
Assembly of the type II secretion machinery of Erwinia chrysanthemi: direct interaction and associated conformational change between OutE, the putative ATP-binding component and the membrane protein OutL
J. Mol. Biol.
289
659-670
1999
Dickeya chrysanthemi
brenda
Van Dijk, K.; Fouts, D.E.; Rehm, A.H.; Hill, A.R.; Collmer, A.; Alfano, J.R.
The Avr (effector) proteins HrmA (HopPsyA) and AvrPto are secreted in culture from Pseudomonas syringae pathovars via the Hrp (type III) protein secretion system in a temperature- and pH-sensitive manner
J. Bacteriol.
181
4790-4797
1999
Pseudomonas syringae
brenda
Schuch, R.; Naurelli, A.T.
The Mxi-Spa type III secretory pathway of Shigella flexneri requires an outer membrane lipoprotein, MxiM, for invasion translocation
Infect. Immun.
67
1982-1991
1999
Shigella flexneri
brenda
Lee, H.M.; Wang, K.C.; Liu, Y.L.; Yew, H.Y.; Chen, L.Y.; Leu, W.M.; Chen, D.C.; Hu, N.T.
Association of the cytoplasmic membrane protein XpsN with the outer membrane protein XpsD in the type II protein secretion apparatus of Xanthomonas campestris pv. campestris
J. Bacteriol.
182
1549-1557
2000
Xanthomonas campestris
brenda
Galan, J.E.; Collmer, A.
Type III secretion machines: bacterial devices for protein delivery into host cells
Science
284
1322-1328
1999
Bordetella bronchiseptica, Chlamydia sp., Escherichia coli, Pantoea agglomerans, Erwinia amylovora, Dickeya chrysanthemi, Pantoea stewartii subsp. stewartii, Salmonella enterica, Pseudomonas aeruginosa, Ralstonia solanacearum, Pseudomonas syringae, Rhizobium sp., Salmonella enterica subsp. enterica serovar Typhimurium, Shigella sp., Xanthomonas campestris, Xanthomonas sp., Yersinia sp.
brenda
Stephens, C.; Mohr, C.; Boyd, C.; Maddock, J.; Gober, J.; Shapiro, L.
Identification of the fliI and fliJ components of the Caulobacter flagellar type III protein secretion system
J. Bacteriol.
179
5355-5365
1997
Caulobacter vibrioides
brenda
Wei, W.; Plovanich-Jones, A.; Deng, W.L.; Jin, Q.L.; Collmer, A.; Huang, H.C.; He, S.Y.
The gene coding for the Hrp pilus structural protein is required for type III secretion of Hrp and Avr proteins in Pseudomonas syringae pv. tomato
Proc. Natl. Acad. Sci. USA
97
2247-2252
2000
Pseudomonas syringae
brenda
Kubori, T.; Matsushima, Y.; Nakamura, D.; Uralil, J.; Lara-Tejero, M.; Sukhan, A.; Galan, J.E.; Aizawa, S.I.
Supramolecular structure of the Salmonella typhimurium type III protein secretion system
Science
280
602-605
1998
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium SJW2941
brenda
Mudgett, M.B.; Chesnokova, O.; Dahlbeck, D.; Clark, E.T.; Rossier, O.; Bonas, U.; Staskawicz, B.J.
Molecular signals required for type III secretion and translocation of the Xanthomonas campestris AvrBs2 protein to pepper plants
Proc. Natl. Acad. Sci. USA
97
13324-13329
2000
Xanthomonas campestris
brenda
Yang, B.; Zhu, W.; Johnson, L.B.; White, F.F.
The virulence factor AvrXa7 of Xanthomonas oryzae pv. oryzae is a type III secretion pathway dependent nuclear-localized double-stranded DNA-binding protein
Proc. Natl. Acad. Sci. USA
97
9807-9812
2000
Xanthomonas oryzae
brenda
Scherer, C.A.; Cooper, E.; Miller, S.I.
The Salmonella type III secretion translocon protein SspC is inserted into the epithelial cell plasma membrane upon infection
Mol. Microbiol.
37
1133-1145
2000
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Thomas, J.D.; Roeeves, P.J.; Salmond, G.P.C.
The general secretion pathway of Erwinia carotovora subsp. carotovora: analysis of the membrane topology of outC and OutF
Microbiology
143
713-720
1997
Pectobacterium carotovorum
brenda
Baker, B.; Zambryski, P.; Staskawicz, B.; Dinesh-Kumar, S.P.
Signaling in plant-microbe interactions
Science
276
726-733
1997
Escherichia coli, Erwinia amylovora, Shigella flexneri, Yersinia enterolytica
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Hueck, C.J.
Type III protein secretion system in bacterial pathogens of animals and plants
Microbiol. Mol. Biol. Rev.
62
379-433
1998
Aeromonas hydrophila, Bordetella pertussis, Chlamydia sp., Escherichia coli, Erwinia sp., Helicobacter pylori, Klebsiella oxytoca, Pseudomonas aeruginosa, Ralstonia solanacearum, Pseudomonas syringae, Salmonella enterica subsp. enterica serovar Typhimurium, Shigella flexneri, Xanthomonas campestris, Yersinia enterolytica, Yersinia sp.
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Savvides, S.N.; Yeo, H.J.; Beck, M.R.; Blaesing, F.; Lurz, R.; Lanka, E.; Buhrdorf, R.; Fischer, W.; Haas, R.; Waksman, G.
VirB11 ATPases are dynamic hexameric assemblies: new insights into bacterial type IV secretion
EMBO J.
22
1969-1980
2003
Helicobacter pylori
brenda
Rossier, O.; Cianciotto, N.P.
Type II protein secretion is a subset of the PilD-dependent processes that facilitate intracellular infection by Legionella pneumophila
Infect. Immun.
69
2092-2098
2001
Legionella pneumophila (Q9AGM7), Legionella pneumophila
brenda
Gauthier, A.; Puente, J.L.; Finlay, B.B.
Secretin of the enteropathogenic Escherichia coli type III secretion system requires components of the type III apparatus for assembly and localization
Infect. Immun.
71
3310-3319
2003
Escherichia coli
brenda
Gauthier, A.; Finlay, B.B.
Translocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli
J. Bacteriol.
185
6747-6755
2003
Escherichia coli
brenda
Akeda, Y.; Galan, J.E.
Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains
J. Bacteriol.
186
2402-2412
2004
Salmonella enterica
brenda
Alegria, M.C.; Docena, C.; Khater, L.; Ramos, C.H.; da Silva, A.C.; Farah, C.S.
New protein-protein interactions identified for the regulatory and structural components and substrates of the type III Secretion system of the phytopathogen Xanthomonas axonopodis Pathovar citri
J. Bacteriol.
186
6186-6197
2004
Xanthomonas axonopodis
brenda
Pozidis, C.; Chalkiadaki, A.; Gomez-Serrano, A.; Stahlberg, H.; Brown, I.; Tampakaki, A.P.; Lustig, A.; Sianidis, G.; Politou, A.S.; Engel, A.; Panopoulos, N.J.; Mansfield, J.; Pugsley, A.P.; Karamanou, S.; Economou, A.
Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization
J. Biol. Chem.
278
25816-25824
2003
Pseudomonas syringae (Q8RK01), Pseudomonas syringae
brenda
Gonzalez-Pedrajo, B.; Fraser, G.M.; Minamino, T.; Macnab, R.M.
Molecular dissection of Salmonella FliH, a regulator of the ATPase Flil and the type III flagellar protein export pathway
Mol. Microbiol.
45
967-982
2002
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Thomas, J.; Stafford, G.P.; Hughes, C.
Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export
Proc. Natl. Acad. Sci. USA
101
3945-3950
2004
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Schoenhofen, I.C.; Li, G.; Strozen, T.G.; Howard, S.P.
Purification and characterization of the N-terminal domain of ExeA: A novel ATPase involved in the type II secretion pathway of Aeromonas hydrophila
J. Bacteriol.
187
6370-6378
2005
Aeromonas hydrophila
brenda
Petnicki-Ocwieja, T.; van Dijk, K.; Alfano, J.R.
The hrpK operon of Pseudomonas syringae pv. tomato DC3000 encodes two proteins secreted by the type III (Hrp) protein secretion system: HopB1 and HrpK, a putative type III translocator
J. Bacteriol.
187
649-663
2005
Pseudomonas syringae
brenda
Blaylock, B.; Riordan, K.E.; Missiakas, D.M.; Schneewind, O.
Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL
J. Bacteriol.
188
3525-3534
2006
Yersinia enterocolitica
brenda
Fu, Z.Q.; Guo, M.; Alfano, J.R.
Pseudomonas syringae HrpJ is a type III secreted protein that is required for plant pathogenesis, injection of effectors, and secretion of the HrpZ1 harpin
J. Bacteriol.
188
6060-6069
2006
Pseudomonas syringae
brenda
Chen, Y.; Shiue, S.; Huang, C.; Chang, J.; Chien, Y.; Hu, N.; Chan, N.
Structure and function of the XpsE N-terminal domain, an essential component of the Xanthomonas campestris Type II secretion system
J. Biol. Chem.
280
42356-42363
2005
Xanthomonas campestris
brenda
Abendroth, J.; Rice, A.E.; McLuskey, K.; Bagdasarian, M.; Hol, W.G.
The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold
J. Mol. Biol.
338
585-596
2004
Vibrio cholerae serotype O1
brenda
Abendroth, J.; Bagdasarian, M.; Sandkvist, M.; Hol, W.G.
The Structure of the cytoplasmic domain of EpsL, an inner membrane component of the type II secretion system of Vibrio cholerae: an unusual member of the actin-like ATPase superfamily
J. Mol. Biol.
344
619-633
2004
Vibrio cholerae serotype O1
brenda
Lopez-Solanilla, E.; Bronstein, P.A.; Schneider, A.R.; Collmer, A.
HopPtoN is a Pseudomonas syringae Hrp (type III secretion system) cysteine protease effector that suppresses pathogen-induced necrosis associated with both compatible and incompatible plant interactions
Mol. Microbiol.
54
353-365
2004
Pseudomonas syringae
brenda
Muller, S.A.; Pozidis, C.; Stone, R.; Meesters, C.; Chami, M.; Engel, A.; Economou, A.; Stahlberg, H.
Double hexameric ring assembly of the type III protein translocase ATPase HrcN
Mol. Microbiol.
61
119-125
2006
Pseudomonas syringae
brenda
Sorg, J.A.; Blaylock, B.; Schneewind, O.
Secretion signal recognition by YscN, the Yersinia type III secretion ATPase
Proc. Natl. Acad. Sci. USA
103
16490-16495
2006
Yersinia enterocolitica
brenda
Andrade, A.; Pardo, J.P.; Espinosa, N.; Perez-Hernandez, G.; Gonzalez-Pedrajo, B.
Enzymatic characterization of the enteropathogenic Escherichia coli type III secretion ATPase EscN
Arch. Biochem. Biophys.
468
121-127
2007
Escherichia coli
brenda
Camberg, J.L.; Johnson, T.L.; Patrick, M.; Abendroth, J.; Hol, W.G.; Sandkvist, M.
Synergistic stimulation of EpsE ATP hydrolysis by EpsL and acidic phospholipids
EMBO J.
26
19-27
2007
Vibrio cholerae serotype O1
brenda
Yamagata, A.; Tainer, J.A.
Hexameric structures of the archaeal secretion ATPase GspE and implications for a universal secretion mechanism
EMBO J.
26
878-890
2007
Archaeoglobus fulgidus
brenda
Wilharm, G.; Dittmann, S.; Schmid, A.; Heesemann, J.
On the role of specific chaperones, the specific ATPase, and the proton motive force in type III secretion
Int. J. Med. Microbiol.
297
27-36
2007
Bacteria, Yersinia sp.
brenda
Chen, Y.; Zhang, X.; Manias, D.; Yeo, H.; Dunny, G.M.; Christie, P.J.
Enterococcus faecalis PcfC, a spatially localized substrate receptor for type IV secretion of the pCF10 transfer intermediate
J. Bacteriol.
190
3632-3645
2008
Enterococcus faecalis
brenda
Pearson, M.M.; Mobley, H.L.
The type III secretion system of Proteus mirabilis HI4320 does not contribute to virulence in the mouse model of ascending urinary tract infection
J. Med. Microbiol.
56
1277-1283
2007
Proteus mirabilis
brenda
Chiang, P.; Sampaleanu, L.M.; Ayers, M.; Pahuta, M.; Howell, P.L.; Burrows, L.L.
Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilB, PilT and PilU
Microbiology
154
114-126
2008
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAK
brenda
Shiue, S.; Chien, I.; Chan, N.; Leu, W.; Hu, N.
Mutation of a key residue in the type II secretion system ATPase uncouples ATP hydrolysis from protein translocation
Mol. Microbiol.
65
401-412
2007
Xanthomonas campestris
brenda
Zarivach, R.; Vuckovic, M.; Deng, W.; Finlay, B.B.; Strynadka, N.C.
Structural analysis of a prototypical ATPase from the type III secretion system
Nat. Struct. Mol. Biol.
14
131-137
2007
Escherichia coli
brenda
Minamino, T.; Namba, K.
Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export
Nature
451
485-488
2008
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Savvides, S.N.
Secretion Superfamily ATPases Swing Big
Structure
15
255-257
2007
Bacteria
brenda
Clausen, M.; Koomey, M.; Maier, B.
Dynamics of type IV pili is controlled by switching between multiple states
Biophys. J.
96
1169-1177
2009
Xanthomonas campestris
brenda
Okabe, M.; Minamino, T.; Imada, K.; Namba, K.; Kihara, M.
Role of the N-terminal domain of FliI ATPase in bacterial flagellar protein export
FEBS Lett.
583
743-748
2009
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium SJW1103
brenda
Jakovljevic, V.; Leonardy, S.; Hoppert, M.; Sogaard-Andersen, L.
PilB and PilT are ATPases acting antagonistically in type IV pilus function in Myxococcus xanthus
J. Bacteriol.
190
2411-2421
2008
Myxococcus xanthus, Myxococcus xanthus DK 1622
brenda
Riordan, K.E.; Sorg, J.A.; Berube, B.J.; Schneewind, O.
Impassable YscP substrates and their impact on the Yersinia enterocolitica type III secretion pathway
J. Bacteriol.
190
6204-6216
2008
Yersinia enterocolitica
brenda
Stone, C.B.; Johnson, D.L.; Bulir, D.C.; Gilchrist, J.D.; Mahony, J.B.
Characterization of the putative type III secretion ATPase CdsN (Cpn0707) of Chlamydophila pneumoniae
J. Bacteriol.
190
6580-6588
2008
Chlamydia pneumoniae, Chlamydia pneumoniae CWL-029 / ATCC VR1310
brenda
Lorenz, C.; Buettner, D.
Functional characterization of the type III secretion ATPase HrcN from the plant pathogen Xanthomonas campestris pv. vesicatoria
J. Bacteriol.
191
1414-1428
2009
Xanthomonas campestris
brenda
Rodgers, L.; Gamez, A.; Riek, R.; Ghosh, P.
The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE
J. Biol. Chem.
283
20857-20863
2008
Yersinia pseudotuberculosis
brenda
Gazi, A.D.; Bastaki, M.; Charova, S.N.; Gkougkoulia, E.A.; Kapellios, E.A.; Panopoulos, N.J.; Kokkinidis, M.
Evidence for a coiled-coil interaction mode of disordered proteins from bacterial type III secretion systems
J. Biol. Chem.
283
34062-34068
2008
Pseudomonas syringae
brenda
Riordan, K.E.; Schneewind, O.
YscU cleavage and the assembly of Yersinia type III secretion machine complexes
Mol. Microbiol.
68
1485-1501
2008
Yersinia sp.
brenda
Paul, K.; Erhardt, M.; Hirano, T.; Blair, D.F.; Hughes, K.T.
Energy source of flagellar type III secretion
Nature
451
489-492
2008
Salmonella enterica
brenda
Wagner, S.; Stenta, M.; Metzger, L.C.; Dal Peraro, M.; Cornelis, G.R.
Length control of the injectisome needle requires only one molecule of Yop secretion protein P (YscP)
Proc. Natl. Acad. Sci. USA
107
13860-13865
2010
Yersinia sp.
brenda
Stone, C.; Bulir, D.; Gilchrist, J.; Toor, R.; Mahony, J.
Interactions between flagellar and type III secretion proteins in Chlamydia pneumoniae
BMC Microbiol.
10
18
2010
Chlamydia pneumoniae (A0A0F7X030)
brenda
Boonyom, R.; Karavolos, M.H.; Bulmer, D.M.; Khan, C.M.
Salmonella pathogenicity island 1 (SPI-1) type III secretion of SopD involves N- and C-terminal signals and direct binding to the InvC ATPase
Microbiology
156
1805-1814
2010
Salmonella enterica
brenda
Swietnicki, W.; Carmany, D.; Retford, M.; Guelta, M.; Dorsey, R.; Bozue, J.; Lee, M.; Olson, M.
Identification of small-molecule inhibitors of Yersinia pestis type III secretion system YscN ATPase
PLoS ONE
6
e19716
2011
Yersinia pestis
brenda
Minamino, T.
Protein export through the bacterial flagellar type III export pathway
Biochim. Biophys. Acta
1843
1642-1648
2014
Aquifex aeolicus (O67531), Salmonella enterica (Q8Z5R8)
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Chen, L.; Ai, X.; Portaliou, A.G.; Minetti, C.A.; Remeta, D.P.; Economou, A.; Kalodimos, C.G.
Substrate-activated conformational switch on chaperones encodes a targeting signal in type III secretion
Cell Rep.
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709-715
2013
Escherichia coli
brenda
Gong, L.; Lai, S.C.; Treerat, P.; Prescott, M.; Adler, B.; Boyce, J.D.; Devenish, R.J.
Burkholderia pseudomallei type III secretion system cluster 3 ATPase BsaS, a chemotherapeutic target for small-molecule ATPase inhibitors
Infect. Immun.
83
1276-1285
2015
Burkholderia pseudomallei (Q63K25), Burkholderia pseudomallei, Burkholderia pseudomallei K96243 (Q63K25)
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Aguilera, L.; Ferreira, E.; Gimenez, R.; Fernandez, F.J.; Taules, M.; Aguilar, J.; Vega, M.C.; Badia, J.; Baldoma, L.
Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli
Int. J. Biochem. Cell Biol.
44
955-962
2012
Escherichia coli (B7UMA6), Escherichia coli
brenda
Dash, R.; Hosen, S.M.; Sultana, T.; Junaid, M.; Majumder, M.; Ishat, I.A.; Uddin, M.M.
Computational analysis and binding site identification of type III secretion system ATPase from Pseudomonas aeruginosa
Interdiscip. Sci.
8
403-411
2015
Pseudomonas aeruginosa (A0A7L5EWH5), Pseudomonas aeruginosa
brenda
Ripoll-Rozada, J.; Zunzunegui, S.; de la Cruz, F.; Arechaga, I.; Cabezon, E.
Functional interactions of VirB11 traffic ATPases with VirB4 and VirD4 molecular motors in type IV secretion systems
J. Bacteriol.
195
4195-4201
2013
Agrobacterium tumefaciens (P07169), Agrobacterium tumefaciens C58 / ATCC 33970 (P07169)
brenda
Kato, J.; Lefebre, M.; Galan, J.E.
Structural features reminiscent of ATP-driven protein translocases are essential for the function of a type III secretion-associated ATPase
J. Bacteriol.
197
3007-3014
2015
Salmonella enterica (A0A0H3NGZ8), Salmonella enterica SL1344 (A0A0H3NGZ8)
brenda
Allison, S.E.; Tuinema, B.R.; Everson, E.S.; Sugiman-Marangos, S.; Zhang, K.; Junop, M.S.; Coombes, B.K.
Identification of the docking site between a type III secretion system ATPase and a chaperone for effector cargo
J. Biol. Chem.
289
23734-23744
2014
Salmonella enterica (P74857), Salmonella enterica
brenda
Lu, C.; Korotkov, K.V.; Hol, W.G.
Crystal structure of the full-length ATPase GspE from the Vibrio vulnificus type II secretion system in complex with the cytoplasmic domain of GspL
J. Struct. Biol.
187
223-235
2014
Vibrio vulnificus (Q7MPZ5), Vibrio vulnificus
brenda
Lorenz, C.; Hausner, J.; Buettner, D.
HrcQ provides a docking site for early and late type III secretion substrates from Xanthomonas
PLoS ONE
7
e51063
2012
Xanthomonas campestris, Xanthomonas campestris 85-10
brenda
Chen, Y.L.; Hu, N.T.
Function-related positioning of the type II secretion ATPase of Xanthomonas campestris pv. campestris
PLoS ONE
8
e59123
2013
Xanthomonas campestris (P31742), Xanthomonas campestris
brenda
Chatterjee, R.; Halder, P.K.; Datta, S.
Identification and molecular characterization of YsaL (Ye3555): a novel negative regulator of YsaN ATPase in type three secretion system of enteropathogenic bacteria Yersinia enterocolitica
PLoS ONE
8
e75028
2013
Yersinia enterocolitica (O30438), Yersinia enterocolitica
brenda
Yoshida, Y.; Miki, T.; Ono, S.; Haneda, T.; Ito, M.; Okada, N.
Functional characterization of the type III secretion ATPase SsaN encoded by Salmonella pathogenicity island 2
PLoS ONE
9
e94347
2014
Salmonella enterica (A0A0H3NB84), Salmonella enterica SL1344 (A0A0H3NB84)
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Barta, M.L.; Battaile, K.P.; Lovell, S.; Hefty, P.S.
Hypothetical protein CT398 (CdsZ) interacts with sigma(54) (RpoN)-holoenzyme and the type III secretion export apparatus in Chlamydia trachomatis
Protein Sci.
24
1617-1632
2015
Chlamydia trachomatis, Chlamydia trachomatis (A0A0H3MJU0), Chlamydia trachomatis 434/Bu, Chlamydia trachomatis 434/Bu (A0A0H3MJU0)
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Lu, C.; Turley, S.; Marionni, S.T.; Park, Y.J.; Lee, K.K.; Patrick, M.; Shah, R.; Sandkvist, M.; Bush, M.F.; Hol, W.G.
Hexamers of the type II secretion ATPase GspE from Vibrio cholerae with increased ATPase activity
Structure
21
1707-1717
2013
Vibrio cholerae (P37093), Vibrio cholerae
brenda
Bzdzion, L.; Krezel, H.; Wrzeszcz, K.; Grzegorek, I.; Nowinska, K.; Chodaczek, G.; Swietnicki, W.
Design of small molecule inhibitors of type III secretion system ATPase EscN from enteropathogenic Escherichia coli
Acta Biochim. Pol.
64
49-63
2017
Escherichia coli (B7UMA6), Escherichia coli
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Case, H.B.; Dickenson, N.E.
Kinetic characterization of the Shigella type three secretion system ATPase Spa47 using alpha-32P ATP
Bio Protoc.
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e3074
2018
Shigella flexneri, Shigella flexneri (Q6XVW8)
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Zoltner, M.; Ng, W.M.; Money, J.J.; Fyfe, P.K.; Kneuper, H.; Palmer, T.; Hunter, W.N.
EssC domain structures inform on the elusive translocation channel in the type VII secretion system
Biochem. J.
473
1941-1952
2016
Geobacillus thermodenitrificans (A4IKE7), Geobacillus thermodenitrificans NG80-2 (A4IKE7)
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Case, H.B.; Dickenson, N.E.
MxiN differentially regulates monomeric and oligomeric species of the Shigella type three secretion system ATPase Spa47
Biochemistry
57
2266-2277
2018
Shigella flexneri, Shigella flexneri 2457T
brenda
Arifuzzaman, M.; Mitra, S.; Jahan, S.I.; Jakaria, M.; Abeda, T.; Absar, N.; Dash, R.
A Computational workflow for the identification of the potent inhibitor of type II secretion system traffic ATPase of Pseudomonas aeruginosa
Comput. Biol. Chem.
76
191-201
2018
Pseudomonas aeruginosa
brenda
Kruse, K.; Salzer, R.; Joos, F.; Averhoff, B.
Functional dissection of the three N-terminal general secretory pathway domains and the Walker motifs of the traffic ATPase PilF from Thermus thermophilus
Extremophiles
22
461-471
2018
Thermus thermophilus
brenda
Wang, S.; Liu, X.; Xu, X.; Yang, D.; Wang, D.; Han, X.; Shi, Y.; Tian, M.; Ding, C.; Peng, D.; Yu, S.
Escherichia coli type III secretion system 2 ATPase EivC is involved in the motility and virulence of avian pathogenic Escherichia coli
Front. Microbiol.
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1387
2016
Escherichia coli, Escherichia coli O78
brenda
Aly, K.A.; Anderson, M.; Ohr, R.J.; Missiakas, D.
Isolation of a membrane protein complex for type VII secretion in Staphylococcus aureus
J. Bacteriol.
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e00482-17
2017
Staphylococcus aureus, Staphylococcus aureus USA300 LAC
brenda
Burgess, J.L.; Burgess, R.A.; Morales, Y.; Bouvang, J.M.; Johnson, S.J.; Dickenson, N.E.
Structural and biochemical characterization of Spa47 provides mechanistic insight into type III secretion system ATPase activation and Shigella virulence regulation
J. Biol. Chem.
291
25837-25852
2016
Shigella flexneri (P0A1C1), Shigella flexneri (Q6XVW8), Shigella flexneri 2457T (P0A1C1)
brenda
Terashima, H.; Kawamoto, A.; Tatsumi, C.; Namba, K.; Minamino, T.; Imada, K.
In vitro reconstitution of functional type III protein export and insights into flagellar assembly
mBio
9
e00988-18
2018
Salmonella sp.
brenda
Rule, C.S.; Patrick, M.; Camberg, J.L.; Maricic, N.; Hol, W.G.; Sandkvist, M.
Zinc coordination is essential for the function and activity of the type II secretion ATPase EpsE
MicrobiologyOpen
5
870-882
2016
Vibrio cholerae (P37093), Vibrio cholerae ATCC 39315 (P37093)
brenda
Imada, K.; Minamino, T.; Uchida, Y.; Kinoshita, M.; Namba, K.
Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator
Proc. Natl. Acad. Sci. USA
113
3633-3638
2016
Salmonella enterica
brenda
Burgess, J.L.; Jones, H.B.; Kumar, P.; Toth, R.T.; Middaugh, C.R.; Antony, E.; Dickenson, N.E.
Spa47 is an oligomerization-activated type three secretion system (T3SS) ATPase from Shigella flexneri
Protein Sci.
25
1037-1048
2016
Shigella flexneri, Shigella flexneri 2457T
brenda
Prevost, M.S.; Waksman, G.
X-ray crystal structures of the type IVb secretion system DotB ATPases
Protein Sci.
27
1464-1475
2018
Yersinia pseudotuberculosis (A0A0U1QTI9), Legionella pneumophila (O52185), Legionella pneumophila, Yersinia pseudotuberculosis IP31758 (A0A0U1QTI9)
brenda
Halder, P.K.; Roy, C.; Datta, S.
Structural and functional characterization of type three secretion system ATPase PscN and its regulator PscL from Pseudomonas aeruginosa
Proteins
87
276-288
2018
Pseudomonas aeruginosa (A0A0H2Z9F1), Pseudomonas aeruginosa (O30538), Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2Z9F1)
brenda
Makino, F.; Shen, D.; Kajimura, N.; Kawamoto, A.; Pissaridou, P.; Oswin, H.; Pain, M.; Murillo, I.; Namba, K.; Blocker, A.J.
The architecture of the cytoplasmic region of type III secretion systems
Sci. Rep.
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33341
2016
Salmonella enterica, Shigella flexneri
brenda
Rule, C.S.; Patrick, M.; Sandkvist, M.
Measuring in vitro ATPase activity for enzymatic characterization
J. Vis. Exp.
114
e54305
2016
Vibrio cholerae serotype O1 (P37093), Vibrio cholerae serotype O1 El Tor Inaba N16961 (P37093), Vibrio cholerae serotype O1 ATCC 39315 (P37093)
brenda