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 NamePseudomonas 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 Nameefp
NCBI Gene ID 882605
GenBank Gene Sequence NC_002516.2
Protein Information
Protein NameTranslation elongation factor P(EF-P)
UniProtKB/SwissProt ID Q9HZZ2
NCBI RefSeq NP_251541.1
EMBL-CDSAAG06239
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 ProteinR32
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 DetectionLC/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 Identification2015
Year of Identification Month Wise2015.04
Year of Validation 2015
ReferenceKrafczyk 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]
AuthorKrafczyk 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 Group1 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.
ContactStructural and Computational Biology Unit, EMBL Heidelberg, Heidelberg, Germany.
ReferenceRajkovic 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]
AuthorRajkovic A, Erickson S, Witzky A, Branson OE, Seo J, Gafken PR, Frietas MA, Whitelegge JP, Faull KF, Navarre W, Darwin AJ, Ibba M.
Research Group1 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.
ContactDepartment of Microbiology and Center for RNA Biology, The Ohio State University, Columbus, Ohio, USA (ibba.1@osu.edu)
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-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.
Contact1 Center for Integrated Protein Science Munich, Ludwig-Maximilians-University München, Munich, Germany. 2 Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Martinsried, Germany.