Latest update: September 24, 2018


ProGT46 (SunS)

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ProGT ID ProGT46 (SunS)
ProGT Pathway
Organism Information
Organism NameBacillus subtilis 168
Clinical ImplicationPathogenic
DomainBacteria
PhylumFirmicutes
ClassificationFamily: Bacillaceae
Order: Bacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI)224308
Genome Information
Gene BankAL009126
EMBLAL009126
Gene Information
Gene NamesunS
NCBI Gene ID939123
NCBI Reference SequenceNC_000964.3.
Protein information
Protein NameSunS 
UniProtKB/ SwissProt IDO31986
NCBI Ref SeqNP_390028.1
UniProtKB Sequence>sp|O31986|SUNS_BACSU SPBc2 prophage-derived glycosyltransferase SunS OS=Bacillus subtilis (strain 168) GN=sunS PE=1 SV=1 MKLSDIYLELKKGYADSLLYSDLSLLVNIMEYEKDIDVMSIQSLVAGYEKSDTPTITCGI IVYNESKRIKKCLNSVKDDFNEIIVLDSYSTDDTVDIIKCDFPDVEIKYEKWKNDFSYAR NKIIEYATSEWIYFIDADNLYSKENKGKIAKVARVLEFFSIDCVVSPYIEEYTGHLYSDT RRMFRLNGKVKFHGKVHEEPMNYNHSLPFNFIVNLKVYHNGYNPSENNIKSKTRRNINLT EEMLRLEPENPKWLFFFGRELHLLDKDEEAIDYLKKSINNYKKFNDQRHFIDALVLLCTL LLQRNNYVDLTLYLDILETEYPRCVDVDYFRSAILLVDMQNKLTSLSNMIDEALTDERYS AINTTKDHFKRILISLNIQLENWERVKEISGEIKNDNMKKEIKQYLANSLHNIEHVLKGI EV
EMBL CDSCAB14063.1
Sequence length422 AA
Additional Information1) SunS is the S-glycosyltransferase characterized in vitro which glycosylates SunA peptide with one hexose.
2) SunS recognizes alpha-helix at the N-terminal of the substrate peptide and modifies the Cys residue present in the loop region of SunA.
3) SunS does not modify SunA-C22S mutant, therefore displays high chemoselectivity towards thiol group of a cysteine residue.
Glycosyltransferase Information
Glycosylation TypeS- (Cys) linked 
CAZY FamilyGT2
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential
Donor TypeNucleotide activated suagrs
Donor SpecificityUDP-Glc is the most preferred substrate but it can accept UDP-Gal, UDP-GlcNAc, GDP-Man and UDP-Xyl, though with lesser efficiency.
Glycan Information
Glycan transferredMonosaccharides (Glc, GlcNAc, Gal, Man and Xyl) 
Experimental_strategiesIn vitro 
Acceptor Subtrate Information
Acceptor Substrate name SunA
ProGPdb ID ProGP400
Acceptor Substrate name SunA-C22S
Acceptor Substrate name SunAG21A
Acceptor Substrate name SunAG23A
Acceptor Substrate name SunAG21K
Acceptor Substrate name SunAG23K
Acceptor Substrate name SunAG21F
Acceptor Substrate name SunAG23F
Acceptor Substrate name SunAG21E
Acceptor Substrate name SunAG23E
Acceptor Substrate name SunA-Xa-T19C
Acceptor Substrate name SunA-Xa-∆I20
Acceptor Substrate name SunA-Xa-S16-G17-insAAA
Acceptor Substrate name SunA-Xa-Q13G-A15G
Litrature
Year Of Validation2011 
Reference Oman, T. J., Boettcher, J. M., Wang, H., Okalibe, X. N., & Van Der Donk, W. A. (2011). Sublancin is not a lantibiotic but an S-linked glycopeptide. Nature chemical biology, 7(2), 78.

Authors Oman, T. J., Boettcher, J. M., Wang, H., Okalibe, X. N., & Van Der Donk, W. A.
Research groupsDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Corresponding Author Van Der Donk, W. A.
ContactsDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Reference Wang, H., & Van Der Donk, W. A. (2011). Substrate selectivity of the sublancin S-glycosyltransferase. Journal of the American Chemical Society, 133(41), 16394-16397.

Authors Wang, H., & 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, USA.
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, USA.