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HAMAP rule MF_00141

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General rule information [?]

Accession MF_00141
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 28)
Name EF_P
Scope
Bacteria
Templates P0A6N4 (EFP_ECOLI); Q76G20 (EFP_THET8); P64036 (EFP_SALTY): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
EFP
Protein name
RecName: Full=Elongation factor P;
Short=EF-P;
Gene name
efp

Comments [?]

case <OC:Gammaproteobacteria> and <FT:1>
Function 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.
else
Function 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.
end case
Pathway Protein biosynthesis; polypeptide chain elongation.
case (<OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>) and <FT:1>
Ptm Is beta-lysylated on the epsilon-amino group of #{Lys-34} by the combined action of EpmA and EpmB, and then hydroxylated on the C5 position of the same residue by EpmC. Lysylation is critical for the stimulatory effect of EF-P on peptide-bond formation. The lysylation moiety would extend toward the peptidyltransferase center and stabilize the terminal 3-CCA end of the tRNA. The hydroxylation of the C5 position on #{Lys-34} would allow additional potential stabilizing hydrogen-bond interactions with the P-tRNA.
else case <OC:Gammaproteobacteria> and <FT:1>
Ptm May be beta-lysylated on the epsilon-amino group of #{Lys-34} by the combined action of EpmA and EpmB, and then hydroxylated on the C5 position of the same residue by EpmC (if this protein is present). Lysylation is critical for the stimulatory effect of EF-P on peptide-bond formation. The lysylation moiety may extend toward the peptidyltransferase center and stabilize the terminal 3-CCA end of the tRNA. Hydroxylation of the C5 position on #{Lys-34} may allow additional potential stabilizing hydrogen-bond interactions with the P-tRNA.
end case
Subcellular location Cytoplasm.
Similarity Belongs to the elongation factor P family.

Keywords [?]

Cytoplasm
Protein biosynthesis
Elongation factor
case <OC:Gammaproteobacteria> and <FT:1>
Hydroxylation
end case

Gene Ontology [?]

GO:0003746; Molecular function: translation elongation factor activity.
GO:0006414; Biological process: translational elongation.
GO:0005737; Cellular component: cytoplasm.

Cross-references [?]

Pfam PF01132; EFP; 1;
NCBIfam TIGR00038; Efp; 1;
PROSITE PS01275; EFP; 1;

Features [?]

case <OC:Gammaproteobacteria>
From: EFP_ECOLI (P0A6N4)
Key     From     To       Description   Tag   Condition   FTGroup
MOD_RES (Optional)     34     34       N6-(3,6-diaminohexanoyl)-5-hydroxylysine     K  
end case

Additional information [?]

Size range 184-195 amino acids
Related rules MF_00646 (EFPL supersedes the current rule)
Fusion None
Comments Some organisms appear to have a protein ortholog to EpmA and EpmB but not to EpmC (even among the Enterobacteriales) (e.g. Buchnera), therefore EF-P from these organisms should not have the full modification seen in E.coli.


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