Latest update: September 24, 2018


ProGT65 (ThuS)

Home -> ProGTdb -> Search ProGT_Main -> Display data

ProGT ID ProGT65 (ThuS)
ProGT Pathway
Organism Information
Organism NameBacillus thuringiensis serovar andalousiensis BGSC 4AW1
Clinical ImplicationNon-pathogenic
DomainBacteria
PhylumFirmicutes
ClassificationFamily: Bacillaceae
Order: Bacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI)527032
Genome Information
Gene BankCM000754.1
EMBLCM000754.1
Gene Information
Gene Namebthur0009_56280
Protein information
Protein NameThuS 
UniProtKB/ SwissProt IDC3GCL5
NCBI Ref SeqZP_04099941.1
UniProtKB Sequence>tr|C3GCL5|C3GCL5_BACTU Uncharacterized protein OS=Bacillus thuringiensis serovar andalousiensis BGSC 4AW1 GN=bthur0009_56280 PE=4 SV=1 METLNDLVTRLEHSHPNSSLLKDLSLIQGNEQYNYIKWGDLSNSQNLNELVFQYEKAPYP SITCGILTYNEERCIKRCLDSLGSQFDEILVLDSHSTDNTTKIINRDFPMVKVIYEPWID DFSFHRNKLISLTSSEWIYYIDADNYCVDSTNKFKRVAKLIQFLSIDCIISPMIKEHIGH VYTDNRKMFSVKKGIQFKGKVHEEPINADGSIPQNITVDIMICHDGYDPEVINLSEKNDR NIKLTRQMMEEEPSNPKWLYFYARELHYASEDTHIIETLLIKAIDLYKQSTYKRYQPEAI LLLCSILFQKRQIRKLNEYLDLLEELQPLCSDVNYYRSLILFYDIRLKTGKLLDTLKSSE LENNKYSFIDSSKDHIKALLIELYCSIDDWEGAFTLFDELQSTEARNKFLRRVKTINTHI SKKI
EMBL CDSEEM68351.1
Sequence length424 AA
Additional Information1) ThuS catalyzes both S-glycosylation of the thiol of cysteine and O-glycosylation of the hydroxyl group of serine in peptide substrates in vitro.
2) ThuS catalyzed S-glycosylation is more efficient than O-glycosylation.
3) The biosynthesis of the putative products of the thuS gene cluster were reconstituted in vitro and the resulting S glycosylated peptides thurandacin A and thurandacin B and it exhibits highly selective antimicrobial activity towards B. thuringiensis.
Glycosyltransferase Information
Glycosylation TypeO- (Ser) linked and S- (Cys) linked 
CAZY FamilyGT2
EC Number (BRENDA)2.4.1.119
Mechanism of Glycan TransferSequential
Donor TypeNucleotide activated suagrs
Donor SpecificityUDP-Glc is preferred substrate but it can also accept UDP-GlcNAc, UDP-Gal and UDP-Man.
Glycan Information
Glycan transferredMonosaccharides (Glc, Gal and Man) 
Method of Glycan IndentificationMALDI-TOF-MS
Experimental_strategiesIn vitro 
Acceptor Subtrate Information
Acceptor Substrate name ThuA
ProGPdb ID ProGP458
Acceptor Substrate name ThuA-C28S
Acceptor Substrate name ThuA-S19C
Acceptor Substrate name SunA
Acceptor Substrate name ThuA-CREB
Acceptor Substrate name SunA-CREB
Acceptor Substrate name SunA-syn
Litrature
Year Of Validation2013 
Reference Wang, H., Oman, T. J., Zhang, R., Garcia De Gonzalo, C. V., Zhang, Q., & Van Der Donk, W. A. (2013). The glycosyltransferase involved in thurandacin biosynthesis catalyzes both O-and S-glycosylation. Journal of the American Chemical Society, 136(1), 84-87.

Authors Wang, H., Oman, T. J., Zhang, R., Garcia De Gonzalo, C. V., Zhang, Q., & Van Der Donk, W. A.
Research groupsHoward Hughes Medical Institute and Roger Adams Laboratory, Department of Chemistry, University of Illinois at Urbana-Champaign , 600 South Mathews Avenue, Urbana, Illinois 61801, United States.
Corresponding Author Van Der Donk, W. A.
ContactsHoward Hughes Medical Institute and Roger Adams Laboratory, Department of Chemistry, University of Illinois at Urbana-Champaign , 600 South Mathews Avenue, Urbana, Illinois 61801, United States.