ProGP495 (EF-P)
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ProGP ID | ProGP495 (EF-P) |
Validation Status | Characterized |
Organism Information | |
Organism Name | Pseudomonas aeruginosa strain UCBPP-PA14 |
Domain | Bacteria |
Classification | Family: Pseudomonadaceae Order: Pseudomonadales Class: Gammaproteobacteria Division or phylum: "Proteobacteria" |
Taxonomic ID (NCBI) | 208963 |
Genome Information | |
GenBank | NC_008463.1. |
EMBL | CP000438 |
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 | ef-P |
GenBank Gene Sequence | NC_008463.1 |
Protein Information | |
Protein Name | EF-P |
UniProtKB/SwissProt ID | Q02P14 |
NCBI RefSeq | WP_003090942.1 |
EMBL-CDS | ABJ12091.1 |
UniProtKB Sequence | >sp|Q02P14|EFP_PSEAB Elongation factor P OS=Pseudomonas aeruginosa (strain UCBPP-PA14) GN=efp PE=3 SV=1 MKTAQEFRAGQVANINGAPWVIQKAEFNKSGRNAAVVKMKLKNLLTGAGTETVFKADDKL EPIILDRKEVTYSYFADPLYVFMDSEFNQYEIEKDDLEGVLTFIEDGMTDICEAVFYNDK VISVELPTTIVRQIAYTEPAVRGDTSGKVMKTARLNNGAELQVSAFCEIGDSIEIDTRTG EYKSRVKA |
Sequence length | 188 AA |
Subcellular Location | Cytoplasm |
Glycosylation Status | |
Glycosylation Type | N- (Arg) linked |
Experimentally Validated Glycosite(s) in Full Length Protein | R32 |
Glycosite(s) Annotated Protein Sequence | >sp|Q02P14|EFP_PSEAB Elongation factor P OS=Pseudomonas aeruginosa (strain UCBPP-PA14) GN=efp PE=3 SV=1 MKTAQEFRAGQVANINGAPWVIQKAEFNKSGR*(32)NAAVVKMKLKNLLTGAGTETVFKADDKL EPIILDRKEVTYSYFADPLYVFMDSEFNQYEIEKDDLEGVLTFIEDGMTDICEAVFYNDK VISVELPTTIVRQIAYTEPAVRGDTSGKVMKTARLNNGAELQVSAFCEIGDSIEIDTRTG EYKSRVKA |
Sequence Around Glycosites (21 AA) | IQKAEFNKSGRNAAVVKMKLK |
Glycan Information | |
Glycan Annotation | Monosaccharide (rhamnose) |
Protein Glycosylation linked (PGL) gene(s) | |
OST Gene Name | EarP |
OST ProGT ID | ProGT103 (EarP) |
Literature | |
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-University Munich, Munich, Germany. [2] Department of Biology, Microbiology, LLudwig-Maximilians-University Munich, 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-University Munich, Munich, Germany. [2] Gene Center, Department for Biochemistry, Ludwig-Maximilians-University Munich, 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 of Munich, Munich, Germany. 2 Department of Biology, Microbiology, Ludwig-Maximilians-University of Munich, Martinsried, Germany. |