STRINGSTRING
efp protein (Yersinia pseudotuberculosis) - STRING interaction network
"efp" - Elongation factor P in Yersinia pseudotuberculosis
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
efpElongation factor P; Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation; Belongs to the elongation factor P family (188 aa)    
Predicted Functional Partners:
rplF
50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center (177 aa)
     
 
  0.978
rplR
50S ribosomal protein L18; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance (117 aa)
   
 
  0.977
rpsM
bact_S13- 30S ribosomal protein S13 (118 aa)
   
 
  0.976
rpsC
30S ribosomal protein S3; Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation (232 aa)
   
 
  0.969
rpsD
30S 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 (206 aa)
 
 
  0.968
rpsG
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 (156 aa)
     
 
  0.968
rplE
50S ribosomal protein L5; This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs (179 aa)
     
 
  0.967
rpsS
30S ribosomal protein S19; Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA (92 aa)
     
 
  0.967
rpsQ
30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5’-end of 16S ribosomal RNA (84 aa)
   
      0.966
epmA
Elongation factor P--(R)-beta-lysine ligase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta- lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P (325 aa)
 
 
  0.965
Your Current Organism:
Yersinia pseudotuberculosis
NCBI taxonomy Id: 633
Other names: ATCC 29833, Bacillus pseudotuberkulosis, Bacterium pseudotuberculosis, CCUG 5855, CIP 55.85, DSM 8992, NCTC 10275, Pasteurella pseudotuberculosis, Shigella pseudotuberculosis, Y. pseudotuberculosis, Yersinia pseudotuberculosis
Server load: low (12%) [HD]