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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
cysLRegulator of sulfur assimilation CysL, activates cysJI expression; Transcriptional activator of the cysJI operon which is involved in sulfur assimilation. Also negatively regulates its own transcription. (299 aa)    
Predicted Functional Partners:
lipL
Octanoyl-[GcvH]:protein N-octanoyltransferase; Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.
  
  
 0.929
ywfM
Putative transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter.
  
  
 0.761
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 [...]
      
 0.752
ywdK
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; Belongs to the UPF0382 family.
   
  
 0.568
pta
Phosphotransacetylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
  
 
 0.536
cysJ
Sulfite reductase (flavoprotein alpha-subunit); Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component (Probable).
     
 0.504
cysH
(phospho)adenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite.
      
 0.499
hemQ
Essential component of heme biosynthesis; May function as heme-dependent peroxidase.
  
  
 0.489
bacH
Cyclohexenol-containing tetrahydro-4-hydroxyphenylpyruvate H(4)HPP in bacilysin synthesis; Along with the bacABCDEF operon, BacG is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. BacG catalyzes the stereoselective reduction of exocyclic-delta(3),delta(5)-dihydro-hydroxyphenylpyruvate (ex-H2HPP), adding a pro-S hydride equivalent to C4 position to yield tetrahydro-hydroxyphenylpyruvate (H4HPP). Although the [...]
  
  
 0.475
resD
Two-component response regulator; Member of the two-component regulatory system ResD/ResE. Required for the expression of resA, ctaA, qcrABC and fnr; activation role in global regulation of aerobic and anaerobic respiration.
  
  
 0.468
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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