Latest update: September 24, 2018


ProGT109 (EarP)

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ProGT ID ProGT109 (EarP)
Organism Information
Organism NameNeisseria meningitidis HT1125
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Neisseriaceae
Order: Neisseriales
Class: Betaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)487
Genome Information
Gene BankAE002098.2
EMBLAE002098.2
Gene Information
Gene NameearP
Protein information
Protein NameEarP 
UniProtKB/ SwissProt IDA0A0T7AQA7
NCBI Ref SeqYP_008920709.1
UniProtKB Sequence>tr|A0A0T7AQA7|A0A0T7AQA7_NEIME DUF2331 OS=Neisseria meningitidis GN=efp PE=4 SV=1 MNTPPFVCWIFCKVIDNFGDIGVSLRLARVLHRELGWQVHLWTDDVSALRALCPDLPDVP CVHQDIHVRTWHSDAADIDTAPVPDAVIETFACDLPENVLHIIRRHKPLWLNWEYLSAEE SNERLHLMPSPQEGVQKYFWFMGFSEKSGGLIRERDYRDAVRFDTEALRQRLMLPEKNAP EWLLFGYRSDVWAKWLEMWQQAGSPMTLLLAGAQIIDSLKQSGIIPQNALQNDGDVFQTA SVRLVKIPFVPQQDFDQLLHLADCAVIRGEDSFVRAQLAGKPFFWHIYPQDEHVHLDKLH AFWDKAHGFYTPETASAHRCLSDDLNGGEALSATQRLECWQILQQHQNGWRQGAGAWSRY LFGQPSASEKLAAFVSKHQKIR
EMBL CDSBAU19337
Sequence length382 AA
Function in Native Organism 1) The N. meningitidis efp gene is essential for cell viability.
Potential Application1) EF-P and Arg32 are essential for the viability of the Neisseria meningitidis therefore, EarP should be a promising target for antibacterial drug development specifically against N. meningitidis.
Additional Information1) Rhamnose modified EF-P rescues ribosomes stalled at proline stretches in proteins.
Glycosyltransferase Information
Glycosylation TypeN- (Arg) linked  
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential
Donor TypeNucleotide activated sugars
Donor SpecificitydTDP-l-Rhamnose
Glycan Information
Glycan transferredMonosaccharide (Rha) 
Method of Glycan IndentificationMALDI-TOF MS and ESI-MS
Experimental_strategiesIn vivo and In vitro 
Acceptor Subtrate Information
Acceptor Substrate name EF-P
ProGPdb ID ProGP521
Litrature
Year Of Validation2016 
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.

Authors Yanagisawa, T., Takahashi, H., Suzuki, T., Masuda, A., Dohmae, N., & Yokoyama, S.
Research groupsRIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Corresponding Author Yokoyama, S.
ContactsRIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan