ProGP542 (Translation elongation factor P (EF-P))

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ProGP ID ProGP542 (Translation elongation factor P (EF-P))
Validation Status Characterized
Organism Information
Organism NameNeisseria meningitidis HT1125
Domain Bacteria
Classification Family: Neisseriaceae
Order: Neisseriales
Class: Betaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 909420
Genome Information
GenBank AEQZ01000013.1
EMBL AEQZ01000000
Organism Additional Information Neisseria meningitidis (Gram-negative bacterium) is the causative agent of cerebrospinal meningitis. Sometimes, it crosses the epithelium using its pili to enter the bloodstream. After rapid proliferation, this leads to septicemia. It also crosses the blood-brain barrier to proliferate in the brain.
Gene Information
Gene Nameefp (NMH_0798)
NCBI Gene ID 33952354
GenBank Gene Sequence NZ_CP020452.2
Protein Information
Protein NameTranslation elongation factor P(EF-P)
UniProtKB/SwissProt ID E6MVW0
NCBI RefSeq WP_002219406.1
EMBL-CDSEFV64285.1
UniProtKB Sequence >tr|E6MVW0|E6MVW0_NEIMH Elongation factor P OS=Neisseria meningitidis serogroup B / serotype 15 (strain H44/76) OX=909420 GN=efp PE=1 SV=1 MKTAQELRAGNVFMVGNDPMVVQKTEYIKGGRSSAKVSMKLKNLLTGAASETIYKADDKF DVVILSRKNCTYSYFADPMYVFMDEEFNQYEIEADNIGDALKFIVDGMEDQCEVTFYEGN PISVELPTIIVREVEYTEPAVKGDTSGKVMKTARLVGGTEIQVMSYIENGDKVEIDTRTG EFRKRA
Sequence length 186 AA
Function The EF-P 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. Both EF-P and Arg32 are essential for cell viability.
Protein Structure
PDB ID 5WXK
Glycosylation Status
Glycosylation Type N- (Arg) linked
Experimentally Validated Glycosite(s) in Full Length ProteinR32
Glycosite(s) Annotated Protein Sequence >tr|E6MVW0|E6MVW0_NEIMH Elongation factor P OS=Neisseria meningitidis serogroup B / serotype 15 (strain H44/76) OX=909420 GN=efp PE=1 SV=1 MKTAQELRAGNVFMVGNDPMVVQKTEYIKGGR*(32)SSAKVSMKLKNLLTGAASETIYKADDKF DVVILSRKNCTYSYFADPMYVFMDEEFNQYEIEADNIGDALKFIVDGMEDQCEVTFYEGN PISVELPTIIVREVEYTEPAVKGDTSGKVMKTARLVGGTEIQVMSYIENGDKVEIDTRTG EFRKRA
Technique(s) used for Glycosylation DetectionMALDI-TOF MS and aberrant migration on SDS-PAGE
Technique(s) used for Glycosylated Residue(s) Detection MALDI-TOF MS/MS
Protein Glycosylation- Implication Rhamnosylation activates EF-P which rescues the polyproline-stalled ribosomes.
Glycan Information
Glycan Annotation Cyclic rhamnose moiety
Technique(s) used for Glycan Identification MALDI-TOF MS and HPLC
Literature
Year of Identification2016
Year of Identification Month Wise2016.02
Year of Validation 2016
ReferenceSengoku T, Suzuki T, Dohmae N, Watanabe C, Honma T, Hikida Y, Yamaguchi Y, Takahashi H, Yokoyama S, Yanagisawa T. (2018) Structural basis of protein arginine rhamnosylation by glycosyltransferase EarP. Nat Chem Biol., 14(4), 368-374. [PubMed: 29440735]
AuthorSengoku T, Suzuki T, Dohmae N, Watanabe C, Honma T, Hikida Y, Yamaguchi Y, Takahashi H, Yokoyama S, Yanagisawa T.
Research Group1 RIKEN Structural Biology Laboratory, Yokohama, Japan. 2 Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan. 3 Structure-Based Molecular Design Team, RIKEN Center for Life Science Technologies, Yokohama, Japan. 4 Structural Glycobiology Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, RIKEN Global Research Cluster, Wako, Japan. 5 Department of Bacteriology, National Institute of Infectious Disease, Tokyo, Japan. 6 RIKEN Structural Biology Laboratory, Yokohama, Japan. 7 RIKEN Structural Biology Laboratory, Yokohama, Japan.
Corresponding Author Yokoyama S, Yanagisawa T.
ContactDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104.
ReferenceYanagisawa T, Takahashi H, Suzuki T, Masuda A, Dohmae N, Yokoyama S (2016) Neisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell Viability. PLoS One, 11(2), e0147907. [PubMed: 26840407]
AuthorYanagisawa T, Takahashi H, Suzuki T, Masuda A, Dohmae N, Yokoyama S
Research Group1 RIKEN Structural Biology Laboratory, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan. 2 RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan. 3 National Institute of Infectious Disease, Department of Bacteriology, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8640, Japan. 4 RIKEN Center for Sustainable Resource Science (CSRS), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. 5 National Maritime Research Institute, 6-38-1 Shinkawa, Mitaka, Tokyo 181-0004, Japan.
Corresponding Author Yokoyama S
ContactRIKEN Structural Biology Laboratory, Yokohama, Japan.