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 | Family: Pseudomonadaceae Order: Pseudomonadales Class: Gammaproteobacteria Division or phylum: "Proteobacteria" |
| 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 |
| 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. |
| Reference | Krafczyk R, Macošek J, Jagtap PKA, Gast D, Wunder S, Mitra P, Jha AK, Rohr J, Hoffmann-Röder A, Jung K, Hennig J, Lassak J. (2017) Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P. Mbio, 8(5). pii: e01412-17. [PubMed: 28951478] |
| Author | Krafczyk R, Macošek J, Jagtap PKA, Gast D, Wunder S, Mitra P, Jha AK, Rohr J, Hoffmann-Röder A, Jung K, Hennig J, Lassak J. |
| Research Group | 1 Center for integrated Protein Science Munich (CiPSM), Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Munich, Germany. 2 Structural and Computational Biology Unit, EMBL Heidelberg, Heidelberg, Germany. 3 Center for integrated Protein Science Munich (CiPSM), Department of Chemistry, Ludwig-Maximilians-University of München, Munich, Germany. 4 University of Kentucky College of Pharmacy, Lexington, Kentucky, USA. 5 Structural and Computational Biology Unit, EMBL Heidelberg, Heidelberg, Germany. 6 Center for integrated Protein Science Munich (CiPSM), Department of Biology I, Microbiology, Ludwig-Maximilians-University of München, Munich, Germany. |
| Corresponding Author | Hennig J, Lassak J. |
| Contact | Structural and Computational Biology Unit, EMBL Heidelberg, Heidelberg, Germany. |
| Reference | Rajkovic A, Erickson S, Witzky A, Branson OE, Seo J, Gafken PR, Frietas MA, Whitelegge JP, Faull KF, Navarre W, Darwin AJ, Ibba M. (2015) Cyclic Rhamnosylated Elongation Factor P Establishes Antibiotic Resistance in Pseudomonas aeruginosa. MBio, 6(3), e00823. [PubMed: 26060278] |
| Author | Rajkovic A, Erickson S, Witzky A, Branson OE, Seo J, Gafken PR, Frietas MA, Whitelegge JP, Faull KF, Navarre W, Darwin AJ, Ibba M. |
| Research Group | 1 Molecular, Cellular and Developmental Biology Program, The Ohio State University, Columbus, Ohio, USA. 2 Department of Chemistry, The Ohio State University, Columbus, Ohio, USA. 3 Department of Molecular Genetics, The Ohio State University, Columbus, Ohio, USA. 4 Ohio State Biochemistry Program, The Ohio State University, Columbus, Ohio, USA. 5 Department of Microbiology, New York University School of Medicine, New York, New York, USA. 6 Fred Hutchinson Cancer Research Center, Proteomics Facility, Seattle, Washington, USA. 7 Department of Psychiatry and Biobehavioral Sciences, Pasarow Mass Spectrometry Laboratory, Semel Institute for Neuroscience and Human Behavior, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, California, USA. 8 Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada. 9 Department of Microbiology and Center for RNA Biology, The Ohio State University, Columbus, Ohio, USA ibba.1@osu.edu. |
| Corresponding Author | Ibba M. |
| Contact | Department of Microbiology and Center for RNA Biology, The Ohio State University, Columbus, Ohio, USA (ibba.1@osu.edu) |
| Reference | Lassak J, Keilhauer EC, Fürst M, Wuichet K, Gödeke J, Starosta AL, Chen JM, Søgaard-Andersen L, Rohr J, Wilson DN, Häussler S, Mann M, Jung K. (2015) Arginine-rhamnosylation as new strategy to activate translation elongation factor P. Nat Chem Biol., 11(4), 266-70. [PubMed: 25686373] |
| Author | Lassak J, Keilhauer EC, Fürst M, Wuichet K, Gödeke J, Starosta AL, Chen JM, Søgaard-Andersen L, Rohr J, Wilson DN, Häussler S, Mann M, Jung K. |
| Research Group | 1 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. 2 Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, Martinsried, Germany. 3 Max Planck Institute for Terrestrial Microbiology, Marburg, Germany. 4 Institute for Molecular Bacteriology, Twincore, Centre for Clinical and Experimental Infection Research, a joint venture of the Helmholtz Centre of Infection Research and the Hannover Medical School, Hannover, Germany. 5 1] Center for Integrated Protein Science Munich, Ludwig-Maximilians-Universität München, Munich, Germany. [2] Gene Center, Department for Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany. 6 Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, Kentucky, USA. 7 1] Institute for Molecular Bacteriology, Twincore, Centre for Clinical and Experimental Infection Research, a joint venture of the Helmholtz Centre of Infection Research and the Hannover Medical School, Hannover, Germany. [2] Department of Molecular Bacteriology, Helmholtz Centre for Infection Research, Braunschweig, Germany. |
| Corresponding Author | Jung K. |
| Contact | 1 Center for Integrated Protein Science Munich, Ludwig-Maximilians-University München, Munich, Germany. 2 Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Martinsried, Germany. |