InterPro domain: IPR001059

Elongation factor P (EF-P) is a prokaryotic protein translation factor required for efficient peptide bond synthesis on 70S ribosomes from fMet-tRNAfMet [ 1 , 2 ]. 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 [ 3 ].

1. Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction. Biochimie 79, 7-11
2. The gene encoding the elongation factor P protein is essential for viability and is required for protein synthesis. J. Biol. Chem. 272, 32254-9
3. Crystal structure of elongation factor P from Thermus thermophilus HB8. Proc. Natl. Acad. Sci. U.S.A. 101, 9595-600