AC   MF_00141;
DC   Protein; auto
TR   HAMAP; MF_00141; -; 1; level=0
XX
Names: EF_P
XX
ID   EFP
DE   RecName: Full=Elongation factor P;
DE            Short=EF-P;
GN   Name=efp;
XX
case <OC:Gammaproteobacteria> and <FT:1>
CC   -!- FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome
CC       stalling that occurs when 3 or more consecutive Pro residues or the
CC       sequence PPG is present in a protein, possibly by augmenting the
CC       peptidyl transferase activity of the ribosome. Modification of #{Lys-
CC       34} is required for alleviation.
else
CC   -!- FUNCTION: Involved in peptide bond synthesis. Stimulates efficient
CC       translation and peptide-bond synthesis on native or reconstituted 70S
CC       ribosomes in vitro. Probably functions indirectly by altering the
CC       affinity of the ribosome for aminoacyl-tRNA, thus increasing their
CC       reactivity as acceptors for peptidyl transferase.
end case
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
case (<OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>) and <FT:1>
CC   -!- PTM: Is beta-lysylated on the epsilon-amino group of #{Lys-34} by the
CC       combined action of EpmA and EpmB, and then hydroxylated on the C5
CC       position of the same residue by EpmC. Lysylation is critical for the
CC       stimulatory effect of EF-P on peptide-bond formation. The lysylation
CC       moiety would extend toward the peptidyltransferase center and stabilize
CC       the terminal 3-CCA end of the tRNA. The hydroxylation of the C5
CC       position on #{Lys-34} would allow additional potential stabilizing
CC       hydrogen-bond interactions with the P-tRNA.
else case <OC:Gammaproteobacteria> and <FT:1>
CC   -!- PTM: May be beta-lysylated on the epsilon-amino group of #{Lys-34} by
CC       the combined action of EpmA and EpmB, and then hydroxylated on the C5
CC       position of the same residue by EpmC (if this protein is present).
CC       Lysylation is critical for the stimulatory effect of EF-P on peptide-
CC       bond formation. The lysylation moiety may extend toward the
CC       peptidyltransferase center and stabilize the terminal 3-CCA end of the
CC       tRNA. Hydroxylation of the C5 position on #{Lys-34} may allow
CC       additional potential stabilizing hydrogen-bond interactions with the P-
CC       tRNA.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the elongation factor P family.
XX
DR   Pfam; PF01132; EFP; 1; trigger=no
DR   NCBIfam; TIGR00038; Efp; 1; trigger=no
DR   PROSITE; PS01275; EFP; 1; trigger=no
XX
KW   Cytoplasm
KW   Protein biosynthesis
KW   Elongation factor
case <OC:Gammaproteobacteria> and <FT:1>
KW   Hydroxylation
end case
XX
GO   GO:0003746; F:translation elongation factor activity
GO   GO:0006414; P:translational elongation
GO   GO:0005737; C:cytoplasm
XX
FT   From: EFP_ECOLI (P0A6N4)
case <OC:Gammaproteobacteria>
FT   MOD_RES         34
FT                   /note="N6-(3,6-diaminohexanoyl)-5-hydroxylysine"
FT   Optional; Condition: K
end case
XX
Size: 184-195;
Related: MF_00646!;
Template: P0A6N4; Q76G20; P64036;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in CHLMU, CHLPN, CHLTR, LACJO, PARUW, PORGI, RHILO
Plasmid: 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.
XX
# Revision 1.28 2023/06/01
//