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.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
lepAGTP-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. (599 aa)    
Predicted Functional Partners:
lepB
Signal peptidase I; Identified by match to protein family HMM PF00717; match to protein family HMM TIGR02227; Belongs to the peptidase S26 family.
  
 
 0.985
rplM
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.
 
 
 0.982
rpsB
Ribosomal protein S2; Identified by similarity to SP:P02351; match to protein family HMM PF00318; match to protein family HMM TIGR01011; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.974
rpsI
Ribosomal protein S9; Identified by match to protein family HMM PF00380; Belongs to the universal ribosomal protein uS9 family.
 
 
 0.971
rplB
Ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
  
 
 0.968
rpsL
Ribosomal protein S12; With S4 and S5 plays an important role in translational accuracy.
  
 
 0.965
rplT
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.
 
 
 0.963
rpsD
Ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
  
 
 0.961
rpsG
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.
  
 
 0.959
rplC
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.
  
 
 0.957
Your Current Organism:
Pseudomonas protegens
NCBI taxonomy Id: 220664
Other names: P. protegens Pf-5, Pseudomonas fluorescens Pf-5, Pseudomonas protegens Pf-5, Pseudomonas protegens str. Pf-5, Pseudomonas protegens strain Pf-5, Pseudomonas sp. Pf-5
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.