ProGP510 (Translation elongation factor P (EF-P))
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| ProGP ID | ProGP510 (Translation elongation factor P (EF-P)) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Pseudomonas aeruginosa PAO1 |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : gammaproteobacteria Orders : Pseudomonadales Family : Pseudomonadaceae Genus : Pseudomonas Species : aeruginosa Strain : PAO1 |
| Taxonomic ID (NCBI) | 208964 |
| Genome Information | |
| GenBank | AE004091.2 |
| EMBL | AE004091 |
| Organism Additional Information | Pseudomonas aeruginosa is a Gram-negative opportunistic pathogen responsible for nosocomial pneumonia. It possesses a multitude of virulence factors including type IV pili that mediate adhesion to host cells. It is also the major cause of mortality among cystic fibrosis (CF) patients. |
| Gene Information | |
| Gene Name | efp |
| NCBI Gene ID | 882605 |
| GenBank Gene Sequence | NC_002516.2 |
| Protein Information | |
| Protein Name | Translation elongation factor P(EF-P) |
| UniProtKB/SwissProt ID | Q9HZZ2 |
| NCBI RefSeq | NP_251541.1 |
| EMBL-CDS | AAG06239 |
| UniProtKB Sequence | >sp|Q9HZZ2|EFP_PSEAE Elongation factor P OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=efp PE=1 SV=1 MKTAQEFRAGQVANINGAPWVIQKAEFNKSGRNAAVVKMKLKNLLTGAGTETVFKADDKL EPIILDRKEVTYSYFADPLYVFMDSEFNQYEIEKDDLEGVLTFIEDGMTDICEAVFYNDK VISVELPTTIVRQIAYTEPAVRGDTSGKVMKTARLNNGAELQVSAFCEIGDSIEIDTRTG EYKSRVKA |
| Sequence length | 188 AA |
| Function | EF-P, a ubiquitous bacterial protein that is required for the synthesis of poly-proline motifs during translation, is a translation elongation factor that is necessary for pathogenicity. Activated EF-P binds at polyproline-stalled ribosomes and stimulates Pro-Pro peptide bond formation, thereby alleviating translational arrest. |
| Protein Structure | |
| PDB ID | 3OYY |
| Glycosylation Status | |
| Glycosylation Type | N- (Arg) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | R32 |
| Glycosite(s) Annotated Protein Sequence | >sp|Q9HZZ2|EFP_PSEAE Elongation factor P OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=efp PE=1 SV=1 MKTAQEFRAGQVANINGAPWVIQKAEFNKSGR*(32)NAAVVKMKLKNLLTGAGTETVFKADDKL EPIILDRKEVTYSYFADPLYVFMDSEFNQYEIEKDDLEGVLTFIEDGMTDICEAVFYNDK VISVELPTTIVRQIAYTEPAVRGDTSGKVMKTARLNNGAELQVSAFCEIGDSIEIDTRTG EYKSRVKA |
| Sequence Around Glycosites (21 AA) | IQKAEFNKSGRNAAVVKMKLK |
| Technique(s) used for Glycosylation Detection | LC/MS/MS |
| Technique(s) used for Glycosylated Residue(s) Detection | LC/MS/MS |
| Protein Glycosylation- Implication | This modification activates EF-P and is crucial for bacterial fitness (key role in gene expression and survival) as well as pathogenicity. It is the first instance where a glycosylated side chain of a translation elongation factor is shown as essential for function. |
| 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. Both EF-P and corresponding EarP are essential for pathogenicity. This forms the basis for targeted-inhibitor design against P. aeruginosa infection. Glycosyltransferase EarP attaches a cyclic rhamnose moiety onto EF-P at the amine position of its highly conserved R34 residue. |
| Literature | |
| Year of Identification | 2015 |
| Year of Identification Month Wise | 2015.04 |
| Year of Validation | 2015 |
| Reference | Krafczyk, R., Macošek, J., Jagtap, P.K.A., Gast, D., Wunder, S., Mitra, P., Jha, A.K., Rohr, J., Hoffmann-Röder, A., Jung, K. and Hennig, J., 2017. Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P. MBio, 8(5), pp.e01412-17. |
| Corresponding Author | Jürgen Lassak Janosch Hennig |
| Contact | Center for integrated Protein Science Munich (CiPSM), Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Munich, Germany Structural and Computational Biology Unit, EMBL Heidelberg, Heidelberg, Germany |
| Reference | Rajkovic, A., Erickson, S., Witzky, A., Branson, O.E., Seo, J., Gafken, P.R., Frietas, M.A., Whitelegge, J.P., Faull, K.F., Navarre, W. and Darwin, A.J., 2015. Cyclic rhamnosylated elongation factor P establishes antibiotic resistance in Pseudomonas aeruginosa. MBio, 6(3), pp.e00823-15. |
| Corresponding Author | Michael Ibba |
| Contact | Department of Microbiology and Center for RNA Biology, The Ohio State University, Columbus, Ohio, USA ibba |
| 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. |