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
tilStRNA(Ile)-lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family. (472 aa)    
Predicted Functional Partners:
hpt
Hypoxanthine phosphoribosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the purine/pyrimidine phosphoribosyltransferase family.
 
  
 0.982
AJF84354.1
(2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.790
thiS
Thiamine biosynthesis protein ThiS; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.788
pth
peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family.
 
  
 0.748
mfd
Transcription-repair coupling factor; Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site; In the C-terminal section; belongs to the helicase family. RecG subfamily.
 
  
 0.731
ftsH
Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.
     
 0.707
mnmE
tRNA modification GTPase; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
 
   
 0.693
AJF85429.1
Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.680
prmC
SAM-dependent methyltransferase; 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.
 
  
 0.653
yeaZ
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.638
Your Current Organism:
Bacillus atrophaeus
NCBI taxonomy Id: 1452
Other names: ATCC 49337, B. atrophaeus, Bacillus atriphaeus, Bacillus sp. S2 BC-2, Bacillus subtilis DSM 2277, Bacillus subtilis DSM 675, CCUG 28524, CIP 107159, DSM 7264, IFO 15539, JCM 9070, LMG 16797, LMG:16797, NBRC 15539, NRRL NRS-213
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.