STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
cheAChemotactic two-component sensor histidine kinase; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to CheB, CheY or CheV. (672 aa)    
Predicted Functional Partners:
cheV
Coupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis.
 0.999
fliY
Flagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family.
 
  
 0.999
cheY
Regulator of chemotaxis and motility; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming.
 
 0.999
cheB
Methyl-accepting chemotaxis proteins (MCP)-glutamate methylesterase; Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. B.subtilis has an effective methylation-independent adaptation system but must utilize the methylation system for adaptation to high concentrations of attractant; Belongs to the CheB family.
 0.999
cheW
Modulation of CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheV and CheW are involved in the coupling of the methyl-accepting chemoreceptors to the central two- component kinase CheA; they are both necessary for efficient chemotaxis.
 
 0.999
cheC
CheY-P phosphatase CheC; Involved in restoring normal CheY-P levels following the addition of attractant by increasing the rate of CheY-P hydrolysis. Is only 6% as active as FliY, which indicates that CheC may function after addition of an attractant to cope with increased levels of CheY-P whereas FliY may function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P. In addition, it was shown to prevent methylation of the methyl-accepting chemotaxis proteins (MCPs). Inhibits CheD.
 
 0.999
cheD
Chemoreceptor glutamine deamidase CheD; Deamidates 'Gln-593' and 'Gln-594' of the chemoreceptor McpA. In addition, deamidates other chemoreceptors, including McpB and McpC. CheD-mediated MCP (methyl-accepting chemotaxis proteins) deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase. CheD is absolutely required for a behavioral response mediated by McpC but is not required for the response to asparagine mediated by McpB. CheD is necessary for the generation of wild-type prestimulus CheA autophosphorylation levels. Al [...]
 
  
 0.999
fliM
Flagellar motor switching and energizing component; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliM family.
 
  
 0.998
mcpB
Methyl-accepting chemotaxis protein; Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyl [...]
 
 0.997
mcpC
Methyl-accepting chemotaxis protein; Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyl [...]
 
 0.996
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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