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.
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]
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lipALipoyl 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. (298 aa)    
Predicted Functional Partners:
lplJ
Lipoate-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.
 
 
 0.998
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.
 
 
 0.996
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.
 
 0.992
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.
  
 
 0.970
bioB
Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.
   
  
 0.852
yutI
Putative iron-sulfur scaffold protein; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins.
  
 0.843
miaB
Enzyme for ms(2)i(6)A formation for tRNA modification; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
     
 0.814
lytH
Sporulation-specific L-Ala-D-Glu endopeptidase; L-Ala--D-Glu endopeptidase involved in production of single L-alanine side chains from tetrapeptides in the spore cortex peptidoglycan. Therefore, is required for the endospore cortex maturation.
       0.663
acoC
Acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
 
 
 0.657
odhB
2-oxoglutarate dehydrogenase complex (dihydrolipoamide transsuccinylase, E2 subunit); E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).
 
 
 0.631
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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