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
lepA-2Elongation factor 4; 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. (595 aa)    
Predicted Functional Partners:
rplB
50S 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.
  
 
 
 0.890
rplM
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.
 
 
 0.886
KZL43139.1
50S 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.
 
 
 0.874
rpsB
30S ribosomal protein S2; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.873
rpmA
50S ribosomal protein L27; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bL27 family.
  
   0.859
KZL35672.1
30S ribosomal protein S9; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uS9 family.
  
 
 0.858
rplA
50S ribosomal protein L1; Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
   
 
 0.855
rpsP
30S ribosomal protein S16; Binds to lower part of 30S body where it stabilizes two domains; required for efficient assembly of 30S; in Escherichia coli this protein has nuclease activity; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bS16 family.
 
   0.853
rplO
50S ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
  
 
 
 0.849
prfA
Peptide chain release factor 1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
  
  
 0.847
Your Current Organism:
Lactobacillus collinoides
NCBI taxonomy Id: 33960
Other names: ATCC 27612, CCUG 32259, CIP 103008, DSM 20515, L. collinoides, LMG 9194, LMG:9194
Server load: medium (42%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.