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ProGT89 (CcPglB)

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ProGT ID ProGT89 (CcPglB)
Organism Information
Organism NameCampylobacter coli RM5611
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)1365662
Genome Information
Gene BankNZ_CP007179
Gene Information
Gene NameN218_16655
NCBI Reference SequenceAHK74917.1
Protein information
Protein NameCcPglB 
UniProtKB/ SwissProt IDA0A059HT80
UniProtKB Sequence>tr|A0A059HT80|A0A059HT80_CAMJU Peptide-binding protein OS=Campylobacter jejuni K5 GN=N218_16655 PE=4 SV=1 MLKKEYFKNPTFILLAFIILAYVFSVLCRFYWIFWASEFNEYFFNNELMIISNDGYAFAE GARDMIAGFHQPNDLSYYGSSLSTLTYWFYKITPFSLESIFIYISTFLSSLVVIPLILIA NEYKRPLMGFVAALLASIANSYYNRTMSGYYDTDMLVIVLAMMIVFFMIRLILKKDLLSL ITLPLFVGIYLWWYPSSYTLNVALLGLFFIYTLVFHIKEKTLYMAIILASITLSNIAWFY QSAIIVILFSLFVLQNKRFSFALLGILGLATLVFLILSGGIDPILYQLKFYIFRSDESAN LAQGFMYFNVNQTIQEVESIDLSIFMQRISGSELVFFVSLIGFIFLVRKHKSMILALPML ALGFLALKSGLRFTIYAVPVLALGFGFLMSLLQERKQKNNNTYWWANIGVFIFTFLSLIP MFYHINNYKAPTVFSQNEATKLDELKKIAQREDYVVTWWDYGYPIRYYSDVKTLADGGKH LGKDNFFPSFVLSKDQVAAANMARLSVEYTEKSFYAPLNDILKNDLLQAMMKDYNQNNVD LFLASLSKPDFKINMPKTRDVYIYMPARMSLIFSTVASFSFVDLETGEINKPFTFSAAYP LDVKNGEIYLSNGIALSDDFRSFKINNSTISVNSIIEINSIKQGEYKITPIDDMAQFYIF YLKDSTIPYAQFILMDKTMFNSAYVQMFFLGNYDKNLYDLVINARDAKVFKLKI
EMBL CDSKDA34064.1
Sequence length714 AA
Subcellular LocationMembrane (Integral component of membrane)
Glycosyltransferase Information
Glycosylation TypeN- (Asn) linked 
CAZY FamilyGT66
EC Number (BRENDA)2.4.99.18
Mechanism of Glycan TransferEn bloc
Acceptor specificity Sequon_1Asn-Xaa-Ser
Donor TypeLipid linked sugars
Donor SpecificityUndPP-Heptasaccharide
Glycan Information
Glycan transferredHeptasaccharide 
Method of Glycan IndentificationLC-MS
Experimental_strategiesIn vivo and In vitro 
Acceptor Subtrate Information
Acceptor Substrate name scFv13-R4 DQNAT
Acceptor Substrate name scFv13-R4 AQNAT
Acceptor Substrate name scFv13-R4 EQNAT
Acceptor Substrate name TAMRA-GDQNATAF
Litrature
Year Of Validation2015 
Reference Ollis, A.A., Chai, Y., Natarajan, A., Perregaux, E., Jaroentomeechai, T., Guarino, C., Smith, J., Zhang, S. & DeLisa, M. P. (2015). Substitute sweeteners: diverse bacterial oligosaccharyltransferases with unique N-glycosylation site preferences. Scientific reports, 5, 15237.

Authors Ollis, A.A., Chai, Y., Natarajan, A., Perregaux, E., Jaroentomeechai, T., Guarino, C., Smith, J., Zhang, S. & DeLisa, M. P.
Research groups1 School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY 14853 USA. 2 Department of Microbiology, Cornell University, Ithaca, NY 14853 USA. 3 Comparative Biomedical Sciences, Cornell University, Ithaca, NY 14853 USA. 4 Proteomics and Mass Spectrometry Core Facility, Cornell University, Ithaca, New York
Corresponding Author DeLisa, M. P.
ContactsProteomics and Mass Spectrometry Core Facility, Cornell University, Ithaca, New York 14853.