ProGT121 (EarP)
| ProGT ID | ProGT121 (EarP) |
| Organism Information | |
| Organism Name | Neisseria meningitidis serogroup B/serotype 15 (strain H44/76) |
| Clinical Implication | Pathogenic |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : BetaProteobacteria Orders : Neisseriales Family : Neisseriaceae Genus : Neisseria Species : meningitidis Strain : H44/76 |
| Taxonomic ID (NCBI) | 909420 |
| Genome Information | |
| Gene Bank | AEQZ01000013.1 |
| EMBL | AEQZ01000000 |
| Gene Information | |
| Gene Name | NMH_0797 |
| Protein information | |
| Protein Name | NMH_0797 (EarP) |
| UniProtKB/ SwissProt ID | E6MVV9 |
| NCBI Ref Seq | WP_002225328.1 |
| UniProtKB Sequence | >tr|E6MVV9|E6MVV9_NEIMH Uncharacterized protein OS=Neisseria meningitidis serogroup B / serotype 15 (strain H44/76) OX=909420 GN=NMH_0797 PE=1 SV=1 MNTPPFVCWIFCKVIDNFGDIGVSWRLARVLHRELGWQVHLWTDDVSALRALCPDLPDVP CVHQDIHVRTWHSDAADIDTAPVPDVVIETFACDLPENVLHIIRRHKPLWLNWEYLSAEE SNERLHLMPSPQEGVQKYFWFMGFSEKSGGLIRERDYCEAVRFDTEALRERLMLPEKNAS EWLLFGYRSDVWAKWLEMWRQAGSPMTLLLAGTQIIDSLKQSGVIPQDALQNDGDVFQTA SVRLVKIPFVPQQDFDQLLHLADCAVIRGEDSFVRAQLAGKPFFWHIYPQDENVHLDKLH AFWDKAHGFYTPETVSAHRRLSDDLNGGEALSATQRLECWQTLQQHQNGWRQGAEDWSRY LFGQPSAPEKLAAFVSKHQKIR |
| EMBL CDS | EFV64284.1 |
| Sequence length | 382 AA |
| Potential Application | 1) The structures of EarP in complex with substrates should provide valuable information for the structure-guided development of its inhibitors such as EarP-containing pathogens specific antibacterials. |
| Additional Information | 1) Rhamnosylation by EarP occur through SN2 reaction. 2) EarP very specifically modify its substrate, by recognizing the overall shape and the specific amino acid residues, through various side-chain-specific interactions. |
| Glycosyltransferase Information | |
| Glycosylation Type | N- (Arg) linked |
| CAZY Family | GT104 |
| Mechanism of Glycan Transfer | Sequential |
| Donor Type | dTDP-l-Rhamnose |
| Donor Specificity | Nucleotide activated sugars |
| Glycan Information | |
| Glycan transferred | Monosaccharide (Rha) |
| Acceptor Subtrate Information | |
| Acceptor Substrate name | EF-P |
| ProGPdb ID | ProGP542 |
| Litrature | |
| Year Of Validation | 2018 |
| 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 | 1 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. |