ProGT78 (GtfB)

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ProGT ID ProGT78 (GtfB)
Organism Information
Organism NameStaphylococcus aureus
Clinical ImplicationPathogenic
DomainBacteria
Classification Phylum : Firmicutes
Class : Bacilli
Orders : Bacillales
Family : Staphylococcaceae
Genus : Staphylococcus
Species : aureus
Subspecies : aureus
Strain : USA300_TCH959
Taxonomic ID (NCBI)450394
Genome Information
Gene BankAASB02000025
EMBLAASB02000025 
Gene Information
Gene NamegtfB
NCBI Reference SequenceAASB02000025
Protein information
Protein NameGtfB 
UniProtKB/ SwissProt IDA0A0E1VMC9
NCBI Ref SeqWP_000593162.1
UniProtKB Sequence>tr|A0A0E1VMC9|A0A0E1VMC9_STAA3 Glycosyltransferase stabilizing protein Gtf2 OS=Staphylococcus aureus subsp. aureus USA300_TCH959 GN=gtfB PE=3 SV=1 MIKLFDYFNDHSRKLYESFKASKLEEDLTIVLNDNGFLPDDVISPYQFFADNHNTENMKP RFFNQVTVPAFWEIKGNNNSATINDMGRLRGKIFYQSGERPRIVSRVEWFDDQQRVRFVD YYSKNGIKFAQTVYDLNRKAILKKYMTAEGKEVIYENFVTSDVILDWQGKSYFFPSKLAF VLFFIKQLEITEHHFVINSLALPFSVLYNLPSNGSDVLVWQEQCDGNVPGNMQLMCKGDM KRHCNIIIPDKNEYETMLNIADAKVQSRILQGGYLYNYRSRNRYTKEIVILTNSDQLRNI KVLVETLPDFNFHIAAITEMSDKLMQLDQYANVHLYPSINIDRVNELYQLCDIYLDINEG NEILNAVEQAFDYELLILGYRQTAHHAKVTLSEHLFEHNDEITMESKDQLIQMLESLKDQ QQFRDALLAQKAHAHEISREQFEQVFKQALES
EMBL CDS EES94653.1
Sequence length452 AA
Subcellular LocationMembrane (Integral component of membrane)
Additional Information1) The deletion studies of GtfA and GtfB show that both GtfA-GtfB is involved in the transfer of GlcNAc residues to the peptide backbone of SraP.
Glycosyltransferase Information
Glycosylation TypeO- (Ser/Thr) linked 
CAZY FamilyGT8
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential
Donor TypeUDP-GlcNAc
Donor SpecificityNucleotide activated sugars
Glycan Information
Glycan transferredOligosaccharides  
Method of Glycan IndentificationsWGA blotting
Experimental_strategiesIn vivo 
Acceptor Subtrate Information
Acceptor Substrate name SraP
ProGPdb ID ProGP245
Litrature
Year Of Validation2014 
Reference Li, Y., Huang, X., Li, J., Zeng, J., Zhu, F., Fan, W. and Hu, L., 2014. Both GtfA and GtfB are required for SraP glycosylation in Staphylococcus aureus. Current microbiology, 69(2), pp.121-126.

Corresponding AuthorDepartment of Laboratory Medicine, Union Hospital, Tongji Medical College Huazhong, University of Science and Technology, Wuhan, China.