Latest update: September 24, 2018


ProGT111 (NtPglB)

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ProGT ID ProGT111 (NtPglB)
Organism Information
Organism NameNitratiruptor tergarcus
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Nitratiruptor
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)1069081
Genome Information
Gene BankFWWZ01000001
EMBLFWWZ01000001
Gene Information
Gene NameSAMN05660197_1793
Protein information
Protein NameNtPglB 
UniProtKB/ SwissProt IDA0A1W1WUL2
NCBI Ref SeqWP_084276310.1
UniProtKB Sequence>tr|A0A1W1WUL2|A0A1W1WUL2_9PROT Dolichyl-diphosphooligosaccharide--protein glycosyltransferase OS=Nitratiruptor tergarcus DSM 16512 OX=1069081 GN=SAMN05660197_1793 PE=4 SV=1 MFVKKNTIFLILIVILIAYIFSYVFHIYWIGWASHNPEFFWNNQLMINNVDGYFFGSGAQ KILYHMHLDNPRLLSVWHYGTAVVTAYIVKLLPISLDTAMLYLPPVISSLVVIPIILIGR LYGNLLWGFLSALIASIGWSYYNRTLAGYYDTDMFSAMLPMFILFFLLAAVKYRSLNYIL AASLTVILYPWLYDQGLSIVYAMGIMMFLYLVILYRNEKFSYQAIIIFSFAMMPIFWVLK LFLVFILWYILKTYDTELRKLQIAAGVSVLAFLLLGNVFGIILHKVFSYTSKTEQISGLH FLNVNETVREAGKIPFEVVADRIVGSLLGLVIAVIGYILLLMRNKEFIIALPLWGIGFFA YFGGLRFTVYAVPIAAMSAVYFFFWLSERFEARKVRMAIVSLGTLFVLTPNITHITGCCE KISWLDGIKGFYPLKSYPYLTPTTLLKSEVALLDELNKKSSPKDYAITWWDYGYPIWYYA DVNTLIDGGKHNEDNFLVSKILSTSNQRLAANLAKLSIKVYTDTNKTVAPQLFIKNGKTI NVDKFFTKISSKEYKSPKLNRNIYLILPHRMFNIFPTVTYFSQRNLNTGEVYRREFYYKN RIMQKGNKLYIGQLIVDLQRAIVLIGNQQAPIKSVYIVGIDRSGKSHYKEQKIRNKGINL IINKSFGEAILADDMYLHSTFFQIYLFDKYDPELFEPVVVSPWMKIYRIK
EMBL CDSSMC09967.1
Sequence length710 AA
Subcellular LocationMembrane (Integral component of membrane)
Additional Information1) N. tergarcus OTase enzyme is able to complement C. jejuni PglB in E.coli with relaxed glycan specificities.
2) The N-linked glycan synthesized in N. tergarcus contains an acetylated sugar at the reducing end.
Glycosyltransferase Information
Glycosylation TypeN- (Asn) linked 
CAZY FamilyGT66
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferEn bloc
Acceptor specificity Sequon_1Asp/Glu- Asn-Xaa-Ser/Thr
Donor TypeLipid linked sugars
Glycan Information
Glycan transferredHeptasaccharide, O9 O-antigen with N-acetylglucosamine (GlcNAc) and F. tularensis O-antigen with QuiNAc (2-acetamido-2,6-dideoxy-O-d-glucose). 
Method of Glycan IndentificationMALDI-MS
Experimental_strategiesIn vivo 
Acceptor Subtrate Information
Acceptor Substrate name Cj0114
ProGPdb ID ProGP219
Litrature
Year Of Validation2016 
Reference Mills, D. C., Jervis, A. J., Abouelhadid, S., Yates, L. E., Cuccui, J., Linton, D., & Wren, B. W. (2015). Functional analysis of N-linking oligosaccharyl transferase enzymes encoded by deep-sea vent proteobacteria. Glycobiology, 26(4), 398-409.

Authors Mills, D. C., Jervis, A. J., Abouelhadid, S., Yates, L. E., Cuccui, J., Linton, D., & Wren, B. W.
Research groups1 Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, University of London, Keppel Street, London WC1E 7HT, UK. 2 Faculty of Life Sciences, University of Manchester, Michael Smith Building, Manchester M13 9PT, UK. 3 Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, University of London, Keppel Street, London
Corresponding Author Wren, B. W.
ContactsProteomics and Mass Spectrometry Core Facility, Cornell University, Ithaca, New York 14853.