Latest update: September 24, 2018


ProGT121 (EarP)

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ProGT ID ProGT121 (EarP)
Organism Information
Organism NameNeisseria meningitidis serogroup B / serotype 15 (strain H44/76)
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Neisseriaceae
Order: Neisseriales
Class: Betaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)909420
Genome Information
Gene BankAEQZ01000013.1
EMBLAEQZ01000000
Gene Information
Gene NameNMH_0797
Protein information
Protein NameNMH_0797 (EarP) 
UniProtKB/ SwissProt IDE6MVV9
NCBI Ref SeqWP_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 CDSEFV64284.1
Sequence length382 AA
Potential Application1) 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 Information1) 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 TypeN- (Arg) linked  
CAZY FamilyGT104
Mechanism of Glycan TransferSequential
Donor TypeNucleotide activated sugars
Donor SpecificitydTDP-l-Rhamnose
Glycan Information
Glycan transferredMonosaccharide (Rha) 
Acceptor Subtrate Information
Acceptor Substrate name EF-P
ProGPdb ID ProGP542
Litrature
Year Of Validation2018 
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 groups1 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.
Contacts1 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.