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yneN yneN ccdA ccdA yosR yosR citB citB ydfQ ydfQ yusE yusE skfH skfH bdbC bdbC ytpP ytpP bdbA bdbA bdbB bdbB
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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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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[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.
  
 0.993
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.
 
 
 0.903
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 [...]
  
    0.888
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.
  
 
 0.875
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.
  
  
 0.864
skfH
Sibling killing effect; Required for production of the bacteriocin SkfA.
      
 0.848
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.
   
  
 0.840
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.
  
 
 0.741
bdbA
Bacteriophage SPbeta thiol-disulfide oxidoreductase; Unknown; dispensable for production of the lantibiotic sublancin 168 and for competence for DNA uptake; Belongs to the thioredoxin family.
  
 
 0.738
bdbB
Bacteriophage SPbeta thiol-disulfide oxidoreductase; Important but not absolutely essential for the production of the lantibiotic sublancin 168, it may also be required for the stability of other secreted proteins. Not required for competence for DNA uptake; Belongs to the DsbB family. BdbC subfamily.
   
  
 0.716
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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