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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
motBEnables flagellar motor rotation, linking torque machinery to cell wall; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity). (308 aa)    
Predicted Functional Partners:
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
motA
Proton conductor component of motor; Residues 1 to 295 of 295 are 99.32 pct identical to residues 1 to 295 of 295 from Escherichia coli K-12 Strain MG1655: B1890.
 
 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).
 
  
 0.992
fliG
Flagellar motor switch protein FliG; FliG 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 (By similarity).
 
  
 0.989
fliF
Flagellar biosynthesis; The M ring may be actively involved in energy transduction. Belongs to the FliF family.
 
  
 0.983
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.
 
  
 0.979
flgC
Flagellar biosynthesis, cell-proximal portion of basal-body rod; Residues 1 to 134 of 134 are 100.00 pct identical to residues 1 to 134 of 134 from Escherichia coli K-12 Strain MG1655: B1074; Belongs to the flagella basal body rod proteins family.
 
  
 0.969
flgB
Flagellar biosynthesis, cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
 
  
 0.966
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.
 
  
 0.963
flgK
Flagellar biosynthesis, hook-filament junction protein 1; Residues 1 to 547 of 547 are 99.08 pct identical to residues 1 to 547 of 547 from Escherichia coli K-12 Strain MG1655: B1082.
 
  
 0.959
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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