ProGP495 (EF-P)

Home -> ProGPdb -> Search ProGP -> Display data


ProGP ID ProGP495 (EF-P)
Validation Status Characterized
Organism Information
Organism NamePseudomonas 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 Nameef-P
GenBank Gene Sequence NC_008463.1
Protein Information
Protein NameEF-P
UniProtKB/SwissProt ID Q02P14
NCBI RefSeq WP_003090942.1
EMBL-CDSABJ12091.1
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 LocationCytoplasm
Glycosylation Status
Glycosylation Type N- (Arg) linked
Experimentally Validated Glycosite(s) in Full Length ProteinR32
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 NameEarP
OST ProGT IDProGT103 (EarP)
Literature
ReferenceLassak 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]
AuthorLassak 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 Group1) 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
Contact1 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.