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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(s) Bacteria
Template(s) P0A6N4 (EFP_ECOLI); Q76G20 (EFP_THET8); P64036 (EFP_SALTY); [ Recover all ]
Triggered by HAMAP; MF_00141 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

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

Comments [?]

case <OC:Gammaproteobacteria> and <FT:1>
FUNCTIONInvolved 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
FUNCTIONInvolved 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
PATHWAYProtein biosynthesis; polypeptide chain elongation.
case (<OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>) and <FT:1>
PTMIs 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>
PTMMay 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 LOCATIONCytoplasm.
SIMILARITYBelongs 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 [?]

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

Additional information [?]

Size range 184-195 amino acids
Related rules MF_00646
Fusion Nter: None Cter: 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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