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
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
rocRTranscriptional regulator (NtrC/NifA family); Positive regulator of arginine catabolism. Controls the transcription of the two operons rocABC and rocDEF and probably acts by binding to the corresponding upstream activating sequences. (461 aa)    
Predicted Functional Partners:
sigL
RNA polymerase sigma-54 factor (sigma-L); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of the levanase operon. The open complex (sigma-54 and core RNA polymerase) serves as the receptor for receipt of the melting signal from the remotely bound activator protein LevR for the expression of the levanase operon.
 
   
 0.968
rocG
Glutamate dehydrogenase; Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression [...]
     
 0.913
rocD
Ornithine aminotransferase; Catalyzes the interconversion of ornithine to glutamate semialdehyde. Controls arginine catabolism.
     
 0.885
spo0F
Two-component response regulator; Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation.
 
     0.872
ykuI
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
      
 0.845
argI
Arginase; Involved in the catabolism of arginine. Belongs to the arginase family.
     
 0.772
rocB
Putative N-deacylase involved in arginine and ornithine utilization; Involved in arginine degradative pathway.
  
   
 0.766
rocC
Arginine/ornithine permease; Putative transport protein involved in arginine degradative pathway. Probably transports arginine or ornithine.
      
 0.751
rocA
Delta-1-pyrroline-5 carboxylate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.
  
  
 0.731
gudB
Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...]
     
 0.689
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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