ProGT121 (EarP)
ProGT ID | ProGT121 (EarP) |
Organism Information | |
Organism Name | Neisseria meningitidis serogroup B / serotype 15 (strain H44/76) |
Clinical Implication | Pathogenic |
Domain | Bacteria |
Phylum | Proteobacteria |
Classification | Family: Neisseriaceae Order: Neisseriales Class: Betaproteobacteria Division or phylum: "Proteobacteria" |
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)Â |
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. |
PDB ID | 5WXJ 5WXI 5XVR 5WXK |
Glycosyltransferase Information | |
Glycosylation Type | N- (Arg) linked  |
CAZY Family | GT104 |
Mechanism of Glycan Transfer | Sequential |
Donor Type | Nucleotide activated sugars |
Donor Specificity | dTDP-l-Rhamnose |
Glycan Information | |
Glycan transferred | Monosaccharide (Rha)Â |
Acceptor Subtrate Information | |
Acceptor Substrate name | EF-P |
ProGPdb ID | ProGP542 |
Litrature | |
Year Of Validation | 2018Â |
Reference | Sengoku, 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. Nature chemical biology, 14(4), 368. |
Authors | Sengoku, T., Suzuki, T., Dohmae, N., Watanabe, C., Honma, T., Hikida, Y., Yamaguchi, Y., Takahashi, H., Yokoyama, S. & Yanagisawa, T. |
Research groups | 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. |
Corresponding Author | Yanagisawa, T. |
Contacts | 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. |