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:
some 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
glySGlycyl-trna synthetase (beta subunit); Glycine--tRNA ligase beta subunit; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme (679 aa)    
Predicted Functional Partners:
glyQ
Glycyl-trna synthetase (alpha subunit); Glycine--tRNA ligase alpha subunit; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme
 0.999
ileS
Isoleucyl-trna synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile)
 
  
 0.788
aspS
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn)
  
  
 0.718
yqfL
[pyruvate, water dikinase]-phosphate phosphotransferase / [pyruvate, water dikinase] kinase; Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation
 
     0.712
ccpN
Deor family transcriptional regulator, catabolite repression regulator; Transcription repressor that binds to the promoter of gapB and pckA genes, preventing their expression. Acts as a regulator for catabolite repression of gluconeogenic genes
       0.693
alaS
Alanyl-trna synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain
  
  
 0.650
era
Gtp-binding protein; An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism (By similarity). Binds both GDP and GTP. Complements an E.coli era disruption mutant
 
    0.637
recO
Dna double strand break repair and homologous recombination factor; Plays a role in DNA double-stranded break repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecR. Is recruited to repair centers, foci that are the site of double-strand break(s) after RecN and before RecF; may actively recruit RecF
       0.620
pheT
Phenylalanyl-trna synthetase (beta subunit); Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily
  
  
 0.619
polA
In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity
  
  
 0.605
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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