GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000117

Electronic Gene Ontology annotations created by ARBA machine learning models

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:25686373

Arginine-rhamnosylation as new strategy to activate translation elongation factor P.

EF-P relieves stalled bacterial ribosomes by binding near the peptidyl-transferase center and stimulating peptide-bond formation.

"EF-P, alleviate the stalled ribosomes by binding and stimulating peptide bond formation"
The paper establishes the EarP-arginine type EF-P subfamily and shows that EF-P activity requires post-translational activation.

"activation of EF-P is achieved"
The paper directly connects EF-P and EarP to polyproline-stall rescue.

"EF-P rescues such stalled ribosomes"

PMID:28951478

Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P.

Structural and biochemical work on P. putida EarP/EF-P supports the Arg32 rhamnosylation context for EF-P activity.

"EF-P is rhamnosylated on arginine 32 by the glycosyltransferase EarP"

file:PSEPK/efp/efp-uniprot.txt

UniProtKB reviewed entry for efp

UniProt describes EF-P as a cytoplasmic translation factor involved in peptide-bond synthesis and polypeptide-chain elongation.

file:PSEPK/efp/efp-goa.tsv

QuickGO GOA annotations for efp

file:PSEPK/efp/efp-deep-research-asta.md

Asta retrieval report for efp

Asta retrieval confirmed the supplied UniProt identity context but did not add gene-specific experimental literature beyond the local cached sources.

file:interpro/panther/PTHR30053/PTHR30053-metadata.yaml

PANTHER family metadata for efp