ProGT95 (CuPglB)
ProGT ID | ProGT95 (CuPglB) |
Organism Information | |
Organism Name | Campylobacter upsaliensis RM3195 |
Clinical Implication | Pathogenic |
Domain | Bacteria |
Classification | Phylum : Proteobacteria Class : EpsilonProteobacteria Orders : Campylobacterales Family : Campylobacteraceae Genus : Campylobacter Species : upsaliensis Strain : RM3195 |
Taxonomic ID (NCBI) | 306264 |
Genome Information | |
Gene Bank | AAFJ01000002 |
EMBL | AAFJ01000002 |
Gene Information | |
Gene Name | pglB |
Protein information | |
Protein Name | CuPglB |
UniProtKB/ SwissProt ID | A0A3S4USL4 |
UniProtKB Sequence | >tr|A0A3S4USL4|A0A3S4USL4_CAMUP Dolichyl-diphosphooligosaccharide--protein glycosyltransferase OS=Campylobacter upsaliensis OX=28080 GN=pglB PE=3 SV=1 MKNEAVKNANLRLVFFILLAFGFSVLCRFYWIYWASDFNEYFFNNQLMISSNDGYTFAEG ARDKIAGFHQENDLSFINSSLSILTYVLYKITPFSFESIILYMSVFFSSLIVVPLILIAN ELKRPLMGLFAAFLASIAKSYYNRTMAGYYDTDMLAIVLPMFILYFFIRLVLRKDDFSLL ALPFFMGLYLWWYPSSYTLNVAFIALFTLYVLIYHRKERSFYMAALLCAITLSNIAWFYQ SAIVVLFFAFFMLKNSLFNFKFIALLALGVLVFLVLSGGIDPILYQLKFYLLRSDESASL ARGFAYFNVNLTIQEVESIDLSTFMQRISGSELVFLLSLFGFLWLLKKHKIMLLTLPMLL LGFLALRGGLRFTIYAVPIMALGFGFLSVQLLSLIQKMRPLQETRKLRIFFYGIFPLFVL VLGAYFYFSQSAIYESMGVEFQKSFVSFFVEDTLLFSLLVLALFTPLIFELLWRKKDIRF VCSFYIVGVLLFSLWANLSHIYNYRAHTVFNYNEASILDNLKANVSREDYIVAWWDYGYP IRYYSDVKTLADGGKHLGKDNFFPSFVLSQNPRAAANMARLSVEYTEKSFKTPYNDLLEA MMKDYNFNNVNLFLAALSKEDFTIQTPKTRDIYIYMPSRMAAIFGTVASFSYMSLETGEL ENPFVYSVAYYLGNEDGKLVLSNNMLLHSDFRSFELNGKNYAINSLVEFTSVQQKYYSVV EIDKNAKYYLFHIKDANIPNVQFILMDKAMYESAFVQMFFFGKYDESLYELIVDSKEAKV YKLKL |
Subcellular Location | Membrane (Integral component of membrane) |
Additional Information | 1) It has relaxed substrate specificity towards negatively charged residue in the ?2 position relative to the asparagine as compared to C. jejuni PglB. |
Glycosyltransferase Information | |
Glycosylation Type | N- (Asn) linked |
CAZY Family | GT66 |
EC Number (BRENDA) | 2.4.99.18 |
Mechanism of Glycan Transfer | En bloc |
Acceptor specificity Sequon_1 | Asn-Xaa-Ser |
Donor Type | UndPP-Heptasaccharide |
Donor Specificity | Lipid linked sugars |
Glycan Information | |
Glycan transferred | Heptasaccharide |
Method of Glycan Indentification | LC-MS |
Experimental_strategies | In vivo and In vitro |
Acceptor Subtrate Information | |
Acceptor Substrate name | scFv13-R4 DQNAT |
Acceptor Substrate name | scFv13-R4 AQNAT |
Acceptor Substrate name | scFv13-R4 CQNAT |
Acceptor Substrate name | scFv13-R4 YQNAT |
Acceptor Substrate name | scFv13-R4 WQNAT |
Acceptor Substrate name | scFv13-R4 VQNAT |
Acceptor Substrate name | scFv13-R4 TQNAT |
Acceptor Substrate name | scFv13-R4 SQNAT |
Acceptor Substrate name | scFv13-R4 QQNAT |
Acceptor Substrate name | scFv13-R4 PQNAT |
Acceptor Substrate name | scFv13-R4 NQNAT |
Acceptor Substrate name | scFv13-R4 MQNAT |
Acceptor Substrate name | scFv13-R4 HQNAT |
Acceptor Substrate name | scFv13-R4 GQNAT |
Acceptor Substrate name | scFv13-R4 EQNAT |
Acceptor Substrate name | TAMRA-GDQNATAF |
Litrature | |
Year Of Validation | 2015 |
Reference | Ollis, A.A., Chai, Y., Natarajan, A., Perregaux, E., Jaroentomeechai, T., Guarino, C., Smith, J., Zhang, S. and DeLisa, M.P., 2015. Substitute sweeteners: diverse bacterial oligosaccharyltransferases with unique N-glycosylation site preferences. Scientific reports, 5(1), pp.1-13. |
Corresponding Author | Proteomics and Mass Spectrometry Core Facility, Cornell University, Ithaca, New York 14853. |