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.
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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
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[Homology]
Score
yneNPutative membrane-bound proteins with a thioredoxin-like domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the thioredoxin family. (170 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.
  
 0.994
citB
Aconitate hydratase (aconitase); Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles. Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the rehydration of 2- methyl-cis-aconitate to produce 2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein which plays a role in the regulation of citrate concentration and in the sporulation. To prevent the accumulation of excessive levels of citrate, it binds near the 5' end of the citZ mRNA, decreasing its stability and thereby limiting the conce [...]
  
    0.893
bdbC
Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.
   
  
 0.879
yusE
Putative thiol-disulfide oxidoreductase with thioredoxin domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
  
  
 0.821
yosR
SPbeta phage putative thiol disulfide oxidoreductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin; Belongs to the thioredoxin family.
 
 
 0.812
ydfQ
Putative thioredoxin or thiol-disulfide isomerase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
  
 
 0.787
bdbD
Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation.
     
 0.765
skfH
Sibling killing effect; Required for production of the bacteriocin SkfA.
      
 0.740
ytpP
Putative thiol-disulfide oxidoreductase with thioredoxin domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
  
 
 0.683
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.
 
 
 0.656
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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