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
Databases
Textmining
[Homology]
Score
cheRGlutamate methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. (288 aa)    
Predicted Functional Partners:
cheY
Chemotaxis regulator protein; 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. Shows autophosphatase activity which is enhanced by CheZ.
  
 0.999
cheB
Methyl esterase; 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 (By similarity). Belongs to the CheB family.
  
 0.999
cheM
Methyl accepting chemotaxis protein II; Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar mediates taxis away from the repellents cobalt and nickel. Unlike in E.coli tar, it does not mediates maltose taxis.
 0.999
cheA
Sensory histitine protein 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 either CheB or CheY.
 
  
 0.999
tsr
Serine sensor receptor; similar to E. coli methyl-accepting chemotaxis protein I, serine sensor receptor (AAC77311.1); Blastp hit to AAC77311.1 (551 aa), 86% identity in aa 1 - 551.
 0.999
cheZ
Chemotactic response protein; Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). Acts on free CheY-P. Belongs to the CheZ family.
 
 
 0.998
cheW
Purine-binding chemotaxis protein; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors.
 
  
 0.998
aer
Aerotaxis sensor receptor; Senses cellular redox state or proton motive force; similar to E. coli aerotaxis sensor receptor, flavoprotein (AAC76107.1); Blastp hit to AAC76107.1 (506 aa), 83% identity in aa 1 - 506.
 0.997
trg
Methyl-accepting chemotaxis protein III; Ribose and galactose sensor receptor; similar to E. coli methyl-accepting chemotaxis protein III, ribose sensor receptor (AAC74503.1); Blastp hit to AAC74503.1 (546 aa), 79% identity in aa 6 - 526.
 0.993
tcp
Methyl-accepting transmembrane citrate/phenol chemoreceptor; Acts as a receptor for citrate and mediates taxis away from phenol. Also mediates an attractant response to metal-citrate complexes.
 0.993
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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