STRING protein interaction network
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:
some 3D structure is known or predicted
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
protein homology
Your Input:
Gene Fusion
frrRibosome 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 (185 aa)    
Predicted Functional Partners:
Phenylalanyl-trna synthetase operon leader peptide; One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly
This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8 . In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA . The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation
Large subunit ribosomal protein l27; 50S ribosomal protein L27; Protein involved in structural constituent of ribosome and translation
Protein chain elongation factor ef-g, gtp-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome
Small subunit ribosomal protein s2; Required for ribosomal protein S1 to bind to the 30S subunit
Small subunit ribosomal protein s9; The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. Mutations that decrease this affinity are suppressed in the 70S ribosome
Large subunit 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
Small subunit ribosomal protein s10; Involved in the binding of tRNA to the ribosomes . In addition, in complex with NusB, is involved in the regulation of ribosomal RNA (rRNA) biosynthesis by transcriptional antitermination. S10 binds RNA non-specifically and increases the affinity of NusB for the boxA RNA sequence S10 may constitute the critical antitermination component of the NusB-S10 complex
Small subunit ribosomal protein s5; With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations). The physical location of this protein suggests it may also play a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp
Protein chain elongation factor ef-ts; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. (Microbial infection) Promotes the tRNase activity of CdiA-CT from E.coli strain EC869 (CdiA-CT-EC869); required in vivo but less so in vitro. Probably loads charged tRNA onto EF-Tu, making more ternary GTP-EF-Tu-aa-tRNA complexes. The guanine nucleotide exchange factor capacity of this protein does not seem to be needed as no GTP hydrolysis occurs during tRNA cleava [...]
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
Server load: low (16%) [HD]