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
ychFGTPase YchF; ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner. (363 aa)    
Predicted Functional Partners:
pth
Peptidyl-tRNA hydrolase (aminoacyl-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.
 
  
 0.854
pheT
Phenylalanyl-tRNA synthetase beta chain (Phenylalanine--tRNA ligase beta chain) (PheRS); ATP + L-Phenylalanine + tRNA(Phe) <=> AMP + Pyrophosphate + L-Phenylalanyl-tRNA(Phe); Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.844
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.
 
  
 0.810
guaA
GMP synthase [glutamine-hydrolyzing] (Glutamine amidotransferase) (GMP synthetase); Catalyzes the synthesis of GMP from XMP.
  
  
 0.769
ksgA
Ribosomal RNA small subunit methyltransferase A; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
 
  
 0.765
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.
 
  
 0.750
argS
Arginyl-tRNA synthetase (Arginine--tRNA ligase) (ArgRS); ATP + L-Arginine + tRNA(Arg) <=> AMP + Pyrophosphate + L-Arginyl-tRNA(Arg).
 
  
 0.749
secY
Preprotein translocase SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
   
  
 0.717
pyrG
CTP synthase (UTP--ammonia ligase) (CTP synthetase); Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
   
 
 0.717
rpoC
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
  
 0.713
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
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