ProGT111 (NtPglB)
| ProGT ID | ProGT111 (NtPglB) |
| Organism Information | |
| Organism Name | Nitratiruptor tergarcus |
| Domain | Bacteria |
| Phylum | Proteobacteria |
| Classification | Family: Nitratiruptor Class: Epsilonproteobacteria Division or phylum: "Proteobacteria" |
| Taxonomic ID (NCBI) | 1069081 |
| Genome Information | |
| Gene Bank | FWWZ01000001 |
| EMBL | FWWZ01000001 |
| Gene Information | |
| Gene Name | SAMN05660197_1793 |
| Protein information | |
| Protein Name | NtPglB |
| UniProtKB/ SwissProt ID | A0A1W1WUL2 |
| NCBI Ref Seq | WP_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 CDS | SMC09967.1 |
| Sequence length | 710 AA |
| Subcellular Location | Membrane (Integral component of membrane) |
| Additional Information | 1) 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 Type | N- (Asn) linked |
| CAZY Family | GT66 |
| EC Number (BRENDA) | 2.4.1.- |
| Mechanism of Glycan Transfer | En bloc |
| Acceptor specificity Sequon_1 | Asp/Glu- Asn-Xaa-Ser/Thr |
| Donor Type | Lipid linked sugars |
| Glycan Information | |
| Glycan transferred | Heptasaccharide, 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 Indentification | MALDI-MS |
| Experimental_strategies | In vivo |
| Acceptor Subtrate Information | |
| Acceptor Substrate name | Cj0114 |
| ProGPdb ID | ProGP219 |
| Litrature | |
| Year Of Validation | 2016 |
| 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 groups | 1 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. |
| Contacts | Proteomics and Mass Spectrometry Core Facility, Cornell University, Ithaca, New York 14853. |