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
ychFGTP-dependent nucleic acid-binding protein; ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner. (371 aa)    
Predicted Functional Partners:
glyS
glycyl-tRNA synthetase beta chain; High confidence in function and specificity.
  
  
 0.917
pth
Pth protein; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family.
 
  
 0.842
uvrB
UvrABC system protein B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and [...]
     
 0.820
lepA
GTP-binding protein lepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner.
 
  
 0.802
prfA
Peptide chain release factor 1 (RF-1); Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
 
  
 0.754
rsfS
Conserved hypothetical protein; Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
  
  
 0.725
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP.
  
  
 0.725
pheT-2
phenylalanyl-tRNA synthetase beta chain; High confidence in function and specificity; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.719
metS
MetS protein; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily.
  
  
 0.706
argS
ArgS protein; PF00750: tRNA synthetases class I, TIGR00456: arginyl-tRNA synthetase; High confidence in function and specificity.
 
  
 0.696
Your Current Organism:
Lactococcus lactis
NCBI taxonomy Id: 416870
Other names: L. lactis subsp. cremoris MG1363, Lactococcus lactis subsp. cremoris MG1363, Lactococcus lactis subsp. cremoris str. MG1363, Lactococcus lactis subsp. cremoris strain MG1363
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.