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
lplJLipoate-protein ligase; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to use octanoate as substrate. (331 aa)    
Predicted Functional Partners:
lipA
Lipoyl synthase (lipoic acid synthetase); Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives; Belongs to the radical SAM superfamily. Lipoyl synthase family.
 
 
 0.998
lipL
Octanoyl-[GcvH]:protein N-octanoyltransferase; Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.
 
  
 0.997
gcvH
Glycine cleavage system protein H; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
 
 0.988
yhfI
Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
  
    0.961
lplA
Lipoprotein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type lp: lipoprotein.
      
 0.888
pdhC
Pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit); The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
 
 0.869
pdhD
Dihydrolipoyl dehydrogenase; Catalyzes the oxidation of dihydrolipoamide to lipoamide; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
 
 
 0.867
lpdV
Branched-chain alpha-keto acid dehydrogenase E3 subunit (dihydrolipoamide dehydrogenase); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3); Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
 
 
 0.850
lplB
Putative ABC transporter (permease); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter.
      
 0.848
acoL
Acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
 
 
 0.844
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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