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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
pthpeptidyl-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. (192 aa)    
Predicted Functional Partners:
ychF
GTP-binding protein YchF; ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner.
 
  
 0.871
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.
  
  
 0.834
tilS
tRNA(Ile)-lysidine synthetase, N-terminal domain/tRNA(Ile)-lysidine synthetase, C-terminal domain; 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.
 
  
 0.744
prfA
Bacterial peptide chain release factor 1 (bRF-1); Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
 
  
 0.673
FP2_15050
protein-(glutamine-N5) methyltransferase, release factor-specific; Belongs to the methyltransferase superfamily.
 
  
 0.643
FP2_11220
Hypothetical protein.
     
 0.625
rpmA
LSU ribosomal protein L27P; Belongs to the bacterial ribosomal protein bL27 family.
 
  
 0.624
frr
Ribosome recycling factor; Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another; Belongs to the RRF family.
  
  
 0.615
efp
Translation elongation factor P (EF-P); Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
 
  
 0.581
obg
Obg family GTPase CgtA; An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
 
  
 0.577
Your Current Organism:
Faecalibacterium prausnitzii L26
NCBI taxonomy Id: 718252
Other names: F. prausnitzii L2-6, Faecalibacterium prausnitzii L2-6, Faecalibacterium prausnitzii str. L2-6, Faecalibacterium prausnitzii strain L2-6, butyrate-producing bacterium L2-6
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.