ProGP521 (EF-P)
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| ProGP ID | ProGP521 (EF-P) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Neisseria meningitidis C311 and MC58 |
| Domain | Bacteria |
| Classification | Family: Neisseriaceae Order: Neisseriales Class: Betaproteobacteria Division or phylum: "Proteobacteria" |
| Taxonomic ID (NCBI) | 491 |
| Genome Information | |
| GenBank | AE002098.2 |
| EMBL | AE002098 |
| 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 Name | NMB0937 |
| GenBank Gene Sequence | NC_003112.2 |
| Protein Information | |
| Protein Name | EF-P |
| UniProtKB/SwissProt ID | Q9JZQ8 |
| NCBI RefSeq | NP_273975.1 |
| EMBL-CDS | AAF41343.2 |
| UniProtKB Sequence | >sp|Q9JZQ8|EFP_NEIMB Elongation factor P OS=Neisseria meningitidis serogroup B (strain MC58) GN=efp PE=3 SV=1 MKTAQELRAGNVFMVGNDPMVVQKTEYIKGGRSSAKVSMKLKNLLTGAASETIYKADDKF DVVILSRKNCTYSYFADPMYVFMDEEFNQYEIEADNIGDALKFIVDGMEDQCEVTFYEGN PISVELPTIIVREVEYTEPAVKGDTSGKVMKTARLVGGTEIQVMSYIENGDKVEIDTRTG EFRKRA |
| Sequence length | 186 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 | >tr|X5F6D0|X5F6D0_NEIME Elongation factor P OS=Neisseria meningitidis GN=efp PE=3 SV=1 MKTAQELRAGNVFMVGNDPMVVQKTEYIKGGR*(32)SSAKVSMKLKNLLTGAASETIYKADDKF DVVILSRKNCTYSYFADPMYVFMDEEFNQYEIEADNIGDALKFIVDGMEDQCEVTFYEGN PISVELPTIIVREVEYTEPAVKGDTSGKVMKTARLVGGTEIQVMSYIENGDKIEIDTRTG EFRKRA |
| Sequence Around Glycosites (21 AA) | VQKTEYIKGGRSSAKVSMKLKN |
| Technique(s) used for Glycosylated Residue(s) Detection | MALDI-TOF MS/MS |
| Protein Glycosylation- Implication | The rhamnosylated EF-P(Nm), but not the unmodified EF-P(Nm), restores the growth rate of EF-P-deleted E. coli cells to the wild-type level |
| Glycan Information | |
| Glycan Annotation | Monosaccharide (rhamnose) |
| Protein Glycosylation linked (PGL) gene(s) | |
| OST Gene Name | EarP |
| Literature | |
| Year of Identification | 2016 |
| Year of Identification Month Wise | 2016.3.26 |
| Year of Validation | 2016 |
| Reference | Yanagisawa, T., Takahashi, H., Suzuki, T., Masuda, A., Dohmae, N. and Yokoyama, S., 2016. Neisseria meningitidis translation elongation factor P and its active-site arginine residue are essential for cell viability. PloS one, 11(2), p.e0147907. |
| Corresponding Author | Tatsuo Yanagisawa Shigeyuki Yokoyama |
| Contact | 1. 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. |
| Reference | Yanagisawa 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] |
| Author | Yanagisawa T,Takahashi H, Suzuki T, Masuda A, Dohmae N, Yokoyama S, |
| Research Group | 1 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 |
| Contact | RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan |