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
efpTranslation elongation factor P/translation initiation factor eIF-5A; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity). (187 aa)    
Predicted Functional Partners:
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.
 
 
 0.974
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; Belongs to the universal ribosomal protein uS7 family.
  
 
 0.973
rpsQ
30S RIBOSOMAL PROTEIN S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
  
 
 0.973
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.
  
 
 0.973
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.
 
 
 0.973
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.
 
 
 0.972
rplV
RIBOSOMAL PROTEIN L22; This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).
  
 
 0.970
rpsJ
RIBOSOMAL PROTEIN S10; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family.
   
 
 0.967
rpsL
RIBOSOMAL PROTEIN S12; With S4 and S5 plays an important role in translational accuracy.
  
 
 0.966
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.
  
 
 0.966
Your Current Organism:
Corynebacterium glutamicum
NCBI taxonomy Id: 196627
Other names: C. glutamicum ATCC 13032, Corynebacterium glutamicum ATCC 13032, Corynebacterium glutamicum str. ATCC 13032, Corynebacterium glutamicum strain ATCC 13032
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.