STRINGSTRING
cheY cheY cheZ cheZ cheB cheB cheW cheW cheA cheA fliM fliM cheR cheR tsr tsr fliN fliN tar tar tap tap
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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textmining
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protein homology
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cheYChemotaxis regulator transmits chemoreceptor signals to flagelllar motor components; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation (By similarity). (129 aa)    
Predicted Functional Partners:
cheZ
Chemotactic response; Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
 
 0.999
cheB
Response regulator for chemotaxis (cheA sensor); Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family.
 
 
 0.999
cheW
Positive regulator of CheA protein activity; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. It physically bridges CheA to the MCPs (methyl-accepting chemotaxis proteins) to allow regulated phosphotransfer to CheY and CheB (By similarity).
 0.999
cheA
Sensory transducer kinase between chemo- signal receptors and CheB and CheY; Residues 1 to 654 of 654 are 99.38 pct identical to residues 1 to 654 of 654 from Escherichia coli K-12 Strain MG1655: B1888.
 
 0.999
fliM
Flagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
 
 
 0.999
cheR
Response regulator for chemotaxis; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
 
  
 0.998
tsr
Methyl-accepting chemotaxis protein I, serine sensor receptor; Residues 1 to 554 of 554 are 98.55 pct identical to residues 1 to 551 of 551 from Escherichia coli K-12 Strain MG1655: B4355.
 
 0.998
fliN
Flagellar motor switch protein FliN; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family.
 
 
 0.996
tar
Methyl-accepting chemotaxis protein II, aspartate sensor receptor; Residues 1 to 553 of 553 are 99.63 pct identical to residues 1 to 553 of 553 from Escherichia coli K-12 Strain MG1655: B1886.
 
 0.995
tap
Methyl-accepting chemotaxis protein IV, peptide sensor receptor; Residues 1 to 533 of 533 are 98.87 pct identical to residues 1 to 533 of 533 from Escherichia coli K-12 Strain MG1655: B1885.
 
 0.994
Your Current Organism:
Escherichia coli O157H7 EDL933
NCBI taxonomy Id: 155864
Other names: E. coli O157:H7 str. EDL933, Escherichia coli O157:H7 EDL933, Escherichia coli O157:H7 str. EDL933, Escherichia coli O157:H7 strain EDL933
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