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
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experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
yqhLPutative sulfur transferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (126 aa)    
Predicted Functional Partners:
yqeF
Putative lipoprotein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
     
 0.907
ylbC
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
   
  
 0.902
lipM
Protein octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an intermediate carrier during protein lipoylation. Is also able to catalyze the reverse reaction. Octanoyl-CoA can also act as a substrate although very poorly. Does not display lipoate protein ligase activity, despite its sequence similarity to LplA; Belongs to the octanoyltransferase LipM family.
  
  
 0.802
ygaC
Putative factor; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor; Belongs to the UPF0374 family.
   
  
 0.782
pksJ
Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.
  
 
 0.782
ytwF
Putative sulfur transferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
  
    0.772
skfE
Sporulation killing factor biosynthesis and export; Probably part of the ABC transporter SkfEF involved in the export of the bacteriocin SKF. Probably responsible for energy coupling to the transport system.
     
 0.743
pcrB
Heptaprenylglyceryl-phosphate synthase; Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond- formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP; C15). Ca [...]
   
  
 0.718
yhcV
Putative oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
    
 
 0.680
ytpA
Phospholipase component of bacilysocin synthesis or export; Phospholipase involved in the biosynthesis of the antibiotic bacilysocin. It probably catalyzes the hydrolysis of the 2-sn-acyl moiety of phosphatidylglycerol to produce bacilysocin (lysophosphatidylglycerol). Is also able to catalyze the hydrolysis reaction of one acyl bond in phosphatidylcholine in vitro (actual cleavage point is unknown), resulting in lysophosphatidylcholine.
  
  
 0.663
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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