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ProGT114 (Gtf2)

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ProGT ID ProGT114 (Gtf2)
Organism Information
Organism NameStreptococcus gordonii
Clinical ImplicationPathogenic
DomainBacteria
PhylumFirmicutes
ClassificationFamily: Streptococcaceae
Order: Lactobacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI)1302
Genome Information
Gene BankAY028381
EMBLAY028381
Gene Information
Gene Namegtf2
Protein information
Protein NameGtf2 
UniProtKB/ SwissProt IDQ79T00
UniProtKB Sequence>sp|Q79T00|GTF2_STRGN Glycosyltransferase-stabilizing protein Gtf2 OS=Streptococcus gordonii GN=gtf2 PE=1 SV=1 MIQLFDYYNQETQDLHDSLLAAGYACPTIVIEANGFLPDDMISPYTYFLGDEEGVDHPLF FNQVPVPPFWEITGDHQVARVSDMGEERARIHYASQARGRLVKQVDWLDKKGQLRLSERY NKQGRCFAKTAYKSGQEAFNTTYYSTDGQERIVENHVTGDIILTLDQEPLRIFKSRVDFI RFFLERLDLDLDHILFNSLAYSFLVSHSLTGRAGQDILFWQEPLYDELPGNMQLILDNSQ LRTQTIVIPDLATYEKAMSLAAADQQQKFLHLGYHYDFKRDNYLRKDALILTHSDQIEGL DTLVQSLPQLVFRIAALTEMSPKLLSMLSYKNVVLYQNASLKQIEQLYLESDIYLDINHG GQVLQAVRKAFENNLLILGFEQTLHDRHYIAQQHIFDSSQPAQLASILEEALCGVEQMRS ALQAQGRHANDVPVSLYQETLQSLLGGQHG
EMBL CDSAAS86345.1
Sequence length450 AA
Subcellular LocationMembrane (Integral component of membrane)
Function in Native Organism 1) Deletion of GtfB abolishes adhesin secretion in Streptococcus gordonii.
Additional Information1) GtfB provides the primary binding site for adhesin and then recognize Ser/Thr residues already modified with GlcNAc.
PDB ID 5E9T 5E9U
Glycosyltransferase Information
Glycosylation TypeO- (Ser/Thr) linked 
CAZY FamilyGT8
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential
Donor TypeNucleotide activated sugars
Donor SpecificityUDP-GlcNAc
Glycan Information
Glycan transferredMonosaccharide (GlcNAc) 
Experimental_strategiesIn vivo and In vitro 
Acceptor Subtrate Information
Acceptor Substrate name GspB
ProGPdb ID ProGP229
Litrature
Year Of Validation2016 
Reference Chen, Y., Seepersaud, R., Bensing, B. A., Sullam, P. M., & Rapoport, T. A. (2016). Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis of a bacterial adhesion protein. Proceedings of the National Academy of Sciences, 113(9), E1190-E1199.

Authors Chen, Y., Seepersaud, R., Bensing, B. A., Sullam, P. M., & Rapoport, T. A.
Research groups1 Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115; Department of Cell Biology, Harvard Medical School, Boston 2 San Francisco Veteran Affairs Medical Center, San Francisco, CA 94121; University of California, San Francisco
Corresponding Author Rapoport, T. A.
Contacts1 Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115. 2 Department of Cell Biology, Harvard Medical School, Boston.