Elongation factor P, C-terminal
SMART accession number:SM00841
Description: These nucleic acid binding domains are predominantly found in elongation factor P, where they adopt an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology (PUBMED:15210970).
Interpro abstract (IPR015365):

Elongation factor P (EF-P) stimulates the peptidyltransferase activity in the prokaryotic 70S ribosome. 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 [ (PUBMED:9405429) (PUBMED:16928980) (PUBMED:15922593) (PUBMED:12932732) ]. 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. This entry includes domain III (the second S1 domain of EF_P). Domains II and III of have structural homology to the eIF5A domain C, suggesting that domains II and III evolved by duplication. These domains adopt an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology [ (PUBMED:15210970) ].

GO process:peptide biosynthetic process (GO:0043043)
GO component:cytoplasm (GO:0005737)
Family alignment:
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There are 17994 Elong-fact-P_C domains in 17994 proteins in SMART's nrdb database.

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