Latest update: September 24, 2018


ProGT112 (SlPglB)

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ProGT ID ProGT112 (SlPglB)
Organism Information
Organism NameSulfurovum lithotrophicum
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Helicobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Phylum: Proteobacteria
Taxonomic ID (NCBI)206403
Genome Information
Gene BankCP011308?
EMBLCP011308
Gene Information
Gene NameYH65_01055
NCBI Reference SequenceCP011308
Protein information
Protein NameSlPglB 
UniProtKB/ SwissProt IDA0A0F6Z1U4
NCBI Ref SeqAKF24146.1
UniProtKB Sequence>tr|A0A0F6Z1U4|A0A0F6Z1U4_9PROT Peptide-binding protein OS=Sulfurovum lithotrophicum GN=YH65_01055 PE=4 SV=1 MEKTQGFERRQVLLFMLVAYLFSFAIRMIWVYQFQDNPNFYWNGQLMINTNDGYFFASGA QKVLYGMHLDNPRIPDMWSFGTVALTVLLTKVTPFSLETVILYMPAIISSLVVIPIILIA RLYKGSLWGFFAALLGSIAWSYYNRTMTGYYDTDMFSAMAPMFILYFLMKSTIDFNLKSA LYAALAIAVYPFLYDAGASIVYAMGTLYAVYMIIYHRNEDTTYNSIILVFLALVPFPLAD PYSYIVKIAVLVVLYFILLKSSFEHKKSLFVIGILFLLFMYFGNVFGLILSKISFYTATG TTGAGLHFYGVTQTIREAGKIPFETFANRISGSQIGVILSLVGYIVLVIRHRAFILALPL VGIGVFALWGGLRFTVYAVPVAAMSVIYLFHIITTTVSDKKSIYLVGMTVLTASMLYPNI KHIIQYKVPTVLNKAEVQDLDALRKVSDSKDYVMAWWDYGYPIWFYSDTNTIIDGGKHQN DNFIISKIMQTTSPEVAANLSRLAVETYVSSGYKTIADTLFKNGQKEQLDPNLLLSELEN DAYKLPKKTRNIYLYLPYRMLNIFPTVAVFGNLDLTTGKAERKIAFYPTNAVKNDNGVLQ FSNGIVFDTKKGELFFGKQKVPVKYFIVTQMTKNGETQIQTQPYHAEGQYVVVFMKSYGR FMVMDEETFRSMYVQMFILGKYDKELFEPVVSSPYSRIYKLKR
Sequence length703 AA
Subcellular LocationMembrane (Integral component of membrane)
Additional Information1) S. lithotrophicum OTase enzyme is able to complement C. jejuni PglB in E.coli with relaxed glycan specificities.
2) The N-linked glycan synthesized in S. lithotrophicum contains an acetylated sugar at the reducing end.
Glycosyltransferase Information
Glycosylation TypeN- (Asn) linked 
CAZY FamilyGT66
EC Number (BRENDA)2.4.99.18
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.