ProGP511 (Translation elongation factor P (EF-P))
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| ProGP ID | ProGP511 (Translation elongation factor P (EF-P)) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Shewanella oneidensis MR-1 |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : gammaproteobacteria Orders : Alteromonadales Family : Shewanellaceae Genus : Shewanella Species : oneidensis Strain : MR-1 |
| Taxonomic ID (NCBI) | 211586 |
| Genome Information | |
| GenBank | AE014299.2 |
| EMBL | AE014299.2 |
| Gene Information | |
| Gene Name | efp |
| NCBI Gene ID | 1170052 |
| GenBank Gene Sequence | NC_004347.2 |
| Protein Information | |
| Protein Name | Translation elongation factor P(EF-P) |
| UniProtKB/SwissProt ID | Q8EEP9 |
| NCBI RefSeq | WP_011072320.1 |
| EMBL-CDS | AAN55362 |
| UniProtKB Sequence | >sp|Q8EEP9|EFP_SHEON Elongation factor P OS=Shewanella oneidensis (strain MR-1) OX=211586 GN=efp PE=3 SV=1 MKTAHEVRPGNVIMFEGSPWVVQKTETTRSGRNAAIVKLKLKNLLLNSGTETTFKGEDKI DDIILDRLDCTYSYFADPMYVFMDAEYNQYDVEAENLGDAAAYIVDGMEETCQVTFYDGK AISVEMPTTIVREVIYTEPSARGDTSGKVMKPATITGGGTISVADFVKVGDKIEIDTRTG EFKKRV |
| Sequence length | 186 AA |
| Function | The EF-P is a translation elongation factor that is necessary for pathogenicity of many bacterial species. Activated EF-P binds at polyproline-stalled ribosomes and stimulates Pro-Pro peptide bond formation, thereby alleviating translational arrest. |
| Glycosylation Status | |
| Glycosylation Type | N- (Arg) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | R32 |
| Glycosite(s) Annotated Protein Sequence | >sp|Q8EEP9|EFP_SHEON Elongation factor P OS=Shewanella oneidensis (strain MR-1) OX=211586 GN=efp PE=3 SV=1 MKTAHEVRPGNVIMFEGSPWVVQKTETTRSGR*(32)NAAIVKLKLKNLLLNSGTETTFKGEDKI DDIILDRLDCTYSYFADPMYVFMDAEYNQYDVEAENLGDAAAYIVDGMEETCQVTFYDGK AISVEMPTTIVREVIYTEPSARGDTSGKVMKPATITGGGTISVADFVKVGDKIEIDTRTG EFKKRV |
| Sequence Around Glycosites (21 AA) | VQKTETTRSGRNAAIVKLKLK |
| Technique(s) used for Glycosylation Detection | LC/MS/MS |
| Technique(s) used for Glycosylated Residue(s) Detection | LC/MS/MS |
| Protein Glycosylation- Implication | Rhamnosylation activates EF-P which prevent translational stalling of a gene. |
| Glycan Information | |
| Glycan Annotation | Cyclic rhamnose moiety |
| Protein Glycosylation linked (PGL) gene(s) | |
| Characterized Accessory Gene(s) | EarP rhamnosyltransferase uses dTDP-L-rhamnose as a substrate. |
| Additional Comment | It is the first report of N-linked protein glycosylation on arginine in bacteria. EarP is necessary and sufficient for activation of EF-P. |
| Literature | |
| Year of Identification | 2015 |
| Year of Identification Month Wise | 2015.04 |
| Year of Validation | 2015 |
| Reference | Lassak, J., Keilhauer, E.C., Fürst, M., Wuichet, K., Gödeke, J., Starosta, A.L., Chen, J.M., Søgaard-Andersen, L., Rohr, J., Wilson, D.N. and Häussler, S., 2015. Arginine-rhamnosylation as new strategy to activate translation elongation factor P. Nature chemical biology, 11(4), pp.266-270. |
| Corresponding Author | Kirsten Jung Jürgen Lassak |
| Contact | 1] Center for Integrated Protein Science Munich, Ludwig-Maximilians-Universität München, Munich, Germany. [2] Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Martinsried, Germany. |