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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
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[Homology]
Score
yrhCConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 17056751. (76 aa)    
Predicted Functional Partners:
yrrT
Putative AdoMet-dependent methyltransferase; Could be a S-adenosyl-L-methionine-dependent methyltransferase; Belongs to the methyltransferase superfamily. YrrT family.
  
  
 0.965
mccA
Cystathionine beta-synthase for the reverse transsulfuration pathway; Catalyzes the conversion of O-acetylserine and homocysteine to cystathionine.
  
  
 0.958
mccB
Cystathionine gamma-lyase and homocysteine gamma-lyase for reverse transsulfuration pathway; Catalyzes the conversion of cystathionine to cysteine, and homocysteine to sulfide.
  
  
 0.915
mtnN
Methylthioadenosine / S-adenosylhomocysteine nucleosidase; Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Belongs to the PNP/UDP phosphorylase family. MtnN subfamily.
  
  
 0.912
yezD
Putative paralog of RsbR; Evidence 7: Gene remnant; Product type pr: putative regulator.
   
  
 0.778
cymR
Transcriptional regulator of cysteine biosynthesis; Master repressor of cysteine metabolism in B.subtilis. Controls the expression of genes involved either in cysteine synthesis from sulfide (cysK), sulfonates (ssu), or methionine (mccAB) or in cystine uptake (tcyP). Activity of CymR is positively regulated by CysK in response to cysteine availability. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the Cy [...]
      
 0.560
cysK
Cysteine synthase; Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR- CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.
   
  
 0.537
yrzA
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
  
    0.419
cysE
Serine acetyltransferase; Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS).
      
 0.405
bshBB
Malate N-acetylglucosamine deacetylase (second enzyme); Involved in bacillithiol (BSH) biosynthesis. Catalyzes the second step of the pathway, the deacetylation of N- acetylglucosaminylmalate (GlcNAc-Mal) to glucosamine malate (GlcN-Mal). Belongs to the PIGL family.
      
 0.405
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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