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 NameShewanella oneidensis MR-1
Domain Bacteria
Classification Family: Shewanellaceae
Order: Alteromonadales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 211586
Genome Information
GenBank AE014299.2
EMBL AE014299.2
Gene Information
Gene Nameefp
NCBI Gene ID 1170052
GenBank Gene Sequence NC_004347.2
Protein Information
Protein NameTranslation elongation factor P(EF-P)
UniProtKB/SwissProt ID Q8EEP9
NCBI RefSeq NP_717918.1
EMBL-CDSAAN55362
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 ProteinR32
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 DetectionLC/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
Literature
Year of Identification2015
Year of Identification Month Wise2015.04
Year of Validation 2015
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 Center for Integrated Protein Science Munich, Ludwig-Maximilians-University of München, Munich, Germany. 2 Department of Biology I, Microbiology, Ludwig-Maximilians-University of München, Martinsried, Germany. 3 Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, Martinsried, Germany. 4 Max Planck Institute for Terrestrial Microbiology, Marburg, Germany. 5 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.
Corresponding Author Jung K.
Contact1 Center for Integrated Protein Science Munich, Ludwig-Maximilians-University München, Munich, Germany. 2 2 2 Department of Biology I, Microbiology, Ludwig-Maximilians-University München, Martinsried, Germany.