earP encodes the EF-P arginine rhamnosyltransferase that transfers rhamnose from dTDP-beta-L-rhamnose to a conserved arginine on elongation factor P, activating EF-P for rescue of polyproline-stalled ribosomes.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0106361 protein-arginine rhamnosyltransferase activity | IEA GO_REF:0000002 | ACCEPT | Summary: EarP has protein-arginine rhamnosyltransferase activity toward EF-P. Reason: Retain as the precise molecular function. Supporting Evidence: file:PSEPK/earP/earP-uniprot.txt Protein-arginine rhamnosyltransferase that catalyzes the PMID:28951478 EF-P is rhamnosylated on arginine 32 by the glycosyltransferase EarP file:PSEPK/earP/earP-deep-research-falcon.md EarP performs **protein N-glycosylation on arginine**, specifically transferring a rhamnose to the **guanidino group** of EF-P **Arg32**. file:PSEPK/earP/earP-deep-research-falcon.md EarP uses **dTDP-L-rhamnose** as its sugar donor. |
| GO:0106361 protein-arginine rhamnosyltransferase activity | IDA PMID:28951478 Structural Basis for EarP-Mediated Arginine Glycosylation of... | ACCEPT | Summary: EarP has protein-arginine rhamnosyltransferase activity toward EF-P. Reason: Retain as the precise molecular function. Supporting Evidence: file:PSEPK/earP/earP-uniprot.txt Protein-arginine rhamnosyltransferase that catalyzes the PMID:28951478 EF-P is rhamnosylated on arginine 32 by the glycosyltransferase EarP file:PSEPK/earP/earP-deep-research-falcon.md EarP is described as an **inverting glycosyltransferase** file:PSEPK/earP/earP-deep-research-falcon.md EF-P, specifically the conserved **Arg32** |
| GO:0006414 translational elongation | IMP PMID:25686373 Arginine-rhamnosylation as new strategy to activate translat... | NEW | Summary: EarP-dependent rhamnosylation activates EF-P for rescue of polyproline-stalled ribosomes during translation elongation. Lassak et al. 2015 (the primary discovery paper) established the IMP evidence directly, showing that earP deletion increases doubling time and reduces translation of a polyproline-LacZ reporter about tenfold. Reason: GOA has the precise EarP molecular function but lacks the supported biological-process annotation for EF-P-dependent translational elongation. The IMP is grounded in the Lassak 2015 deletion-mutant phenotype (polyproline reporter), with corroborating in vivo functional data in Krafczyk 2017. Supporting Evidence: PMID:25686373 providing clear experimental evidence that EarP is required for EF-P activity PMID:25686373 EarP is an EF-P arginine rhamnosyltransferase essential for post-translational activation file:PSEPK/earP/earP-uniprot.txt required for EF-P-dependent rescue of polyproline PMID:28951478 alleviates the translational arrest file:PSEPK/earP/earP-deep-research-falcon.md Rhamnosylated EF-P is recruited to stalled ribosomes and promotes peptide-bond formation, especially at problematic **polyproline motifs** |
| GO:0018195 peptidyl-arginine modification | IDA PMID:28951478 Structural Basis for EarP-Mediated Arginine Glycosylation of... | NEW | Summary: EarP rhamnosylates the conserved Arg32 of EF-P, a peptidyl-arginine modification that is the specific biological process EarP itself carries out. Reason: Captures the direct biological process EarP performs (covalent arginine modification of EF-P), complementing the downstream EF-P-dependent translational-elongation role. Supporting Evidence: file:PSEPK/earP/earP-deep-research-falcon.md EarP performs **protein N-glycosylation on arginine**, specifically transferring a rhamnose to the **guanidino group** of EF-P **Arg32**. PMID:28951478 EF-P is rhamnosylated on arginine 32 by the glycosyltransferase EarP |
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Suggested experts: Bacterial translation and EF-P modification experts
Experiment: Compare wild type, earP deletion, and catalytically inactive EarP strains using ribosome profiling and proteomics under conditions enriched for polyproline-containing proteins.
Type: ribosome profiling with EF-P modification analysis
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