Latest update: September 24, 2018


ProGT110 (DfdPglB)

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ProGT ID ProGT110 (DfdPglB)
Organism Information
Organism NameDeferribacter desulfuricans
DomainBacteria
PhylumDeferribacteres
ClassificationFamily: Deferribacteraceae
Order: Deferribacterales
Class: Deferribacteres
Phylum: Deferribacteres
Taxonomic ID (NCBI)639282
Genome Information
Gene BankAP011529
EMBLAP011529
Gene Information
Gene NameDEFDS_0397
Protein information
Protein NameDfdPglB 
UniProtKB/ SwissProt IDD3PBB8
NCBI Ref SeqWP_013007139.1
UniProtKB Sequence>tr|D3PBB8|D3PBB8_DEFDS Uncharacterized protein OS=Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 / SSM1) OX=639282 GN=DEFDS_0397 PE=4 SV=1 MDKKGKFIIVFLLMIGVFVYSAYVRIDQYNKWKEQRSIYFVENYPAMTTLDAYYWLRYAK EYDNGLYYKSDNDTLRYYPDSQPKKRPVPFLSFLIAKLSSFTNNNYYYAGLFLIPILASL FIIPFSLYFYYAGFPFGGIVGSFIGTFSYMYFVRSSMGRVDTDLLNIFFPTLTSLFIFFA AKYENIKKVYFYSALSGLSMLFFYWWYFHPGFTLIYFGVLLVVLFLEKKPKGLILKSAGL FILFSNPLYFFYGIFNLFGFIKNYFTISKENLIGFPNILQTITEAQHKPIKEVLEYIINS PYLSVLGLIIFIIFAALKWRKFLAIAPLFLLGLLAFKSSNRFVMFLAPFAGAGIGMIIDY VVEYVEKNFKKMKPLNIYLVTIAVVVLLCVGLGKLTAKEYVPKPSINPGIIKSFIEMNKK LEKGAIWSWWDYGYAIEDIVGFPVYHDGGSQGSPKTYFIAKSLITDKQSKLYRYISYFDN NGMNEIKEMIEDNKSALDIVKYVDSYKGLPKGNNYVLFTMDMISKFPAYNFIGSYNFNTK TSQKVVVAPLRCQKVEKGVFYCEGNKIDTNSGVINGKIPMKRFDISKDGGLVSSKNYPYE RGYNAELILKGNTIFYLILCDDNFYNSNFNQMYLLGKYDKNLYDEVYNNFPFARVFKVKK
EMBL CDSBAI79891.1
Sequence length660 AA
Subcellular LocationMembrane (Integral component of membrane)
String639282.DEFDS_0397
Additional Information1) D. desulfuricans OTase enzyme is able to complement C. jejuni PglB in E.coli with relaxed glycan specificities.
Glycosyltransferase Information
Glycosylation TypeN- (Asn) linked 
CAZY FamilyGT66
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferEn bloc
Acceptor specificity Sequon_1Asn-Xaa-Ser/Thr
Donor TypeLipid linked sugars
Glycan Information
Glycan transferredO9 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
Acceptor Substrate name Dfd0114
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.