close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
prfAProbable peptide chain release factor 1 (rf-1) protein; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. (360 aa)    
Predicted Functional Partners:
hemK
Probable methylase of polypeptide chain release factors protein; 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.
 
 0.997
rpmA
Probable 50s ribosomal protein l27; Belongs to the bacterial ribosomal protein bL27 family.
 
 
 0.977
rpsG
Probable 30s ribosomal protein s7; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.; Belongs to the universal ribosomal protein uS7 family.
  
 
 0.975
rplM
Probable 50s ribosomal protein l13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
 
 
 0.972
rplT
Probable 550s ribosomal protein l20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
 
 
 0.971
frr
Probable ribosome recycling factor (ribosome-releasing factor) (rrf) protein; 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.
 
 
 0.970
rplQ
Probable 50s ribosomal subunit protein l17.
 
 
 0.961
rplC
Probable 50s ribosomal protein l3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
 
 
 0.961
rplS
Probable 50s ribosomal protein l19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
 
 
 0.958
rplO
Probable 50s ribosomal subunit protein l15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
 
 
 0.954
Your Current Organism:
Ralstonia solanacearum
NCBI taxonomy Id: 267608
Other names: R. solanacearum GMI1000, Ralstonia solanacearum GMI1000, Ralstonia solanacearum str. GMI1000, Ralstonia solanacearum strain GMI1000
Server load: medium (52%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.