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 Name | Neisseria meningitidis HT1125 |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : Betaproteobacteria Orders : Neisseriales Family : Neisseriaceae Genus : Neisseria Species : meningitidis Strain : HT1125 |
| 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 Name | efp (NMH_0798) |
| NCBI Gene ID | 33952354 |
| GenBank Gene Sequence | NZ_CP020452.2 |
| Protein Information | |
| Protein Name | Translation elongation factor P(EF-P) |
| UniProtKB/SwissProt ID | E6MVW0 |
| NCBI RefSeq | WP_002219406.1 |
| EMBL-CDS | EFV64285.1 |
| 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 Protein | R32 |
| 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 Detection | MALDI-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 |
| Protein Glycosylation linked (PGL) gene(s) | |
| Characterized Accessory Gene(s) | The gene NMH_0797 encodes EarP rhamnosyltransferase that uses dTDP-L-rhamnose as a substrate. |
| Additional Comment | The rhamnosyl modification of EF-P(Arg32) is a new antibiotic target |
| Literature | |
| Year of Identification | 2016 |
| Year of Identification Month Wise | 2016.02 |
| Year of Validation | 2016 |
| Reference | Sengoku, T., Suzuki, T., Dohmae, N., Watanabe, C., Honma, T., Hikida, Y., Yamaguchi, Y., Takahashi, H., Yokoyama, S. and Yanagisawa, T., 2018. Structural basis of protein arginine rhamnosylation by glycosyltransferase EarP. Nature Chemical Biology, 14(4), pp.368-374. |
| 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. 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. |