HAMAP rule MF_00141
General rule information
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| 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
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Identifier, protein and gene names
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| Identifier | EFP |
| Protein name | RecName: Full=Elongation factor P; Short=EF-P; |
| Gene name | Name=efp; |
Comments
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| 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
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| Cytoplasm | |
| Protein biosynthesis | |
| Elongation factor | |
| case <OC:Gammaproteobacteria> and <FT:1> | |
| Hydroxylation | |
| end case | |
Gene Ontology
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| GO:0003746; Molecular function:translation elongation factor activity |
| GO:0006414; Biological process:translational elongation |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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Features
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| 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
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| 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. |