Elongation factor P (EF-P) OB domain
SMART accession number:SM01185
Description: -
Interpro abstract (IPR001059):

Elongation factor P (EF-P) is a prokaryotic protein translation factor required for efficient peptide bond synthesis on 70S ribosomes from fMet-tRNAfMet [ (PUBMED:9195040) (PUBMED:9405429) ]. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF-P binds near the streptomycine binding site of the 16S rRNA in the 30S subunit. EF-P interacts with domains 2 and 5 of the 23S rRNA. The L16 ribosomal protein of the 50S or its N-terminal fragment are required for EF-P mediated peptide bond synthesis, whereas L11, L15, and L7/L12 are not required in this reaction, suggesting that EF-P may function at a different ribosomal site than most other translation factors. EF-P is essential for cell viability and is required for protein synthesis. EF-P is mainly present in bacteria. The EF-P homologs in archaea and eukaryotes are the initiation factors aIF5A and eIF5A, respectively.

EF-P has 3 domains (domains I, II, and III). Domains II and III are S1-like domains and have structural homology to the eIF5A domain C, suggesting that domains II and III evolved by duplication. This entry reresents the central domain of elongation factor P and its homologues. It forms an oligonucleotide-binding (OB) fold, though it is not clear if this region is involved in binding nucleic acids [ (PUBMED:15210970) ].

GO process:translational elongation (GO:0006414)
GO function:translation elongation factor activity (GO:0003746)
Family alignment:
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There are 18020 EFP domains in 18020 proteins in SMART's nrdb database.

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