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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ywlGConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 15995210. (180 aa)    
Predicted Functional Partners:
ywlF
Ribose 5-phosphate epimerase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
 
  
 0.996
yfkA
Putative Fe-S oxidoreductase, radical SAM superfamily; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
      
 0.890
yaaO
Putative decarboxylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
      
 0.888
ynbB
Putative C-S lyase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
      
 0.848
gsaB
Glutamate-1-semialdehyde aminotransferase, class III aminotransferase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme.
   
  
 0.755
ytoP
Glutamyl aminopeptidase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.
   
  
 0.684
prmC
Glutamine methylase of release factor 1 (and perhaps others) at a GGQ site; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily.
      0.681
tsaC
tRNA(NNU) t(6)A37 threonylcarbamoyladenosine modification; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Is also able to catalyze the reverse reaction in vitro, i.e. the formation of ATP from TC-AMP and PPi; Belongs to the SUA5 family.
 
    0.597
ymfI
Putative oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family.
      
 0.573
ywlE
Protein-tyrosine-phosphatase; Catalyzes the specific dephosphorylation of phosphoarginine residues in a large number of proteins. Counteracts the protein arginine kinase McsB in vivo. Can dephosphorylate CtsR-P; thus, can restore the DNA-binding ability of the CtsR repressor by reversing the McsB-mediated phosphorylation. Is the only active pArg phosphatase present in B.subtilis. Exhibits almost no activity against pSer, pThr, or pTyr peptides. Appears to play a role in B.subtilis stress resistance. Protein arginine phosphorylation has a physiologically important role and is involved i [...]
  
    0.573
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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