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
yneIPutative response regulator (CheY homolog); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (120 aa)    
Predicted Functional Partners:
ccdA
Cytochrome c-type biogenesis protein CcdA; Required for cytochrome c synthesis and stage V of sporulation. Might transfer reducing equivalents across the cytoplasmic membrane, promoting efficient disulfide bond isomerization of proteins localized on the outer surface of the membrane or in the spore coat.
  
  
 0.995
cheA
Chemotactic 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.
 
 0.994
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.
 
 0.983
ndoA
Endoribonuclease toxin; Toxic component of a type II toxin-antitoxin (TA) system. Specific for 5'-UACAU-3' sequences, cleaving after the first U. Yields cleavage products with 3' phosphate and 5' hydroxyl groups. Cannot digest substrate with a UUdUACAUAA cleavage site. Overexpression is toxic for cell growth (shown in E.coli), probably by inhibiting protein synthesis through the cleavage of single-stranded RNA. The toxicity is reversed by the antitoxin EndoAI. Toxin activity cannot be inhibited by MazE from E.coli. The EndoA-EndoAI complex does not seem to bind its own promoter.
      
 0.980
tlpC
Methyl-accepting chemotaxis protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; receptor.
 
 
 0.974
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.
 
 0.973
tlpA
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 [...]
 
  
 0.973
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 [...]
 
  
 0.973
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 [...]
 
  
 0.972
tlpB
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 [...]
 
  
 0.972
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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