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
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Gene Fusion
Cooccurrence
Coexpression
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[Homology]
Score
trxBThioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. (316 aa)    
Predicted Functional Partners:
trxA
Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
 
 0.999
ahpC
Alkyl hydroperoxide reductase (small subunit); Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
  
 
 0.932
sufS
Cysteine desulfurase; Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40- to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity.
  
 
  0.914
sodA
Superoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family.
  
  
 0.878
tpx
Putative peroxiredoxin; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
  
  
 0.856
ohrR
Transcriptional regulator sensing organic peroxides; Organic peroxide sensor. Represses the expression of the peroxide-inducible gene ohrA by cooperative binding to two inverted repeat elements.
  
  
 0.844
arsC
Thioredoxin-coupled arsenate reductase; Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. In vitro, can dephosphorylate para- nitrophenyl phosphate (pNPP). Belongs to the low molecular weight phosphotyrosine protein phosphatase family. Thioredoxin-coupled ArsC subfamily.
 
  
 0.839
yjbH
Putative thiol management oxidoreductase component; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
  
  
 0.837
bsaA
Putative bacillithiol peroxidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the glutathione peroxidase family.
  
  
 0.836
perR
Transcriptional regulator (Fur family); Hydrogen and organic peroxide sensor. Represses the expression of a regulon of peroxide-inducible genes such as katA, ahpC, ahpF, the heme biosynthesis operon (hemAXCDBL), fur, perR, zosA and mrgA; Belongs to the Fur family.
  
  
 0.777
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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