efp encodes elongation factor P, a cytoplasmic bacterial translation factor that stimulates peptide-bond formation during elongation and helps rescue ribosomes stalled on difficult motifs such as polyproline sequences. In pseudomonads, EF-P function depends on EarP-mediated rhamnosylation of a conserved arginine.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003746 translation elongation factor activity | IEA GO_REF:0000120 | ACCEPT | Summary: EF-P is correctly annotated as a translation elongation factor. Reason: UniProt describes EF-P as involved in peptide-bond synthesis and efficient translation on 70S ribosomes, and the cached literature supports EF-P as the bacterial factor that relieves stalled ribosomes by stimulating peptide-bond formation. Supporting Evidence: file:PSEPK/efp/efp-uniprot.txt Involved in peptide bond synthesis. file:PSEPK/efp/efp-uniprot.txt Stimulates efficient PMID:25686373 EF-P, alleviate the stalled ribosomes by binding and stimulating peptide bond formation |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: Cytoplasm is the expected location for EF-P action on bacterial ribosomes. Reason: UniProt assigns EF-P to the cytoplasm, consistent with its activity on cytoplasmic 70S ribosomes during translation elongation. Supporting Evidence: file:PSEPK/efp/efp-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm PMID:25686373 Ribosomes translate an mRNA sequence into a polypeptide chain. |
| GO:0005829 cytosol | IEA GO_REF:0000117 | ACCEPT | Summary: Cytosol is compatible with EF-P's soluble translation-factor role. Reason: The ARBA cytosol annotation is consistent with UniProt cytoplasm localization and with EF-P acting on cytosolic bacterial ribosomes; no evidence suggests membrane, periplasmic, or secreted localization. Supporting Evidence: file:PSEPK/efp/efp-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0006414 translational elongation | IEA GO_REF:0000120 | ACCEPT | Summary: EF-P functions during translational elongation. Reason: UniProt places EF-P in the protein-biosynthesis/polypeptide-chain-elongation pathway, and the primary literature identifies EF-P as a bacterial elongation factor that stimulates peptide-bond formation at stalled ribosomes. Supporting Evidence: file:PSEPK/efp/efp-uniprot.txt PATHWAY: Protein biosynthesis; polypeptide chain elongation. PMID:25686373 activation of EF-P is achieved |
| GO:0006417 regulation of translation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Regulation of translation is a valid but broad consequence of EF-P activity. Reason: EF-P changes translational output for stall-prone motifs, but its direct curated role is elongation-factor activity and rescue of stalled ribosomes rather than a generic regulatory program. Supporting Evidence: PMID:25686373 EF-P rescues such stalled ribosomes |
| GO:0043043 peptide biosynthetic process | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Peptide biosynthetic process is a correct broad parent of the EF-P elongation role. Reason: EF-P participates in polypeptide-chain elongation and peptide-bond synthesis, but the more informative core process annotations are translational elongation and stalled cytosolic ribosome rescue. Supporting Evidence: file:PSEPK/efp/efp-uniprot.txt Involved in peptide bond synthesis. |
| GO:0072344 rescue of stalled cytosolic ribosome | IEA GO_REF:0000117 | ACCEPT | Summary: EF-P is appropriately annotated to rescue of stalled cytosolic ribosomes. Reason: EF-P is the bacterial factor that rescues polyproline-stalled ribosomes, and UniProt specifically notes that EarP-dependent Arg32 rhamnosylation is required for EF-P function and rescue of polyproline-stalled ribosomes. Supporting Evidence: file:PSEPK/efp/efp-uniprot.txt required for EF-P function and rescue of polyproline stalled ribosomes. PMID:25686373 EF-P rescues such stalled ribosomes |
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Download this section (compressed HTML)Q: Which KT2440 proteins and growth conditions are most dependent on EarP-modified EF-P for efficient translation?
Experiment: Compare ribosome profiling and proteomics in wild-type, efp-deficient, and EarP-modification-defective backgrounds to identify KT2440 translation stalls that depend on rhamnosylated EF-P.
Type: ribosome profiling with proteomics
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