ProGT33 (GtfA)

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ProGT ID ProGT33 (GtfA)
Organism Information
Organism NameStreptococcus agalactiae serotype III (strain NEM316)
Clinical ImplicationPathogenic
DomainBacteria
Classification Phylum : Firmicutes
Class : Bacilli
Orders : Lactobacillales
Family : Streptococcaceae
Genus : Streptococcus
Species : agalactiae
Strain : NEM316
Taxonomic ID (NCBI)211110
Genome Information
Gene BankNC_004368.1
EMBLAL766851
Gene Information
Gene Namegbs1515
NCBI Reference SequenceCAD47174
Protein information
UniProtKB/ SwissProt IDQ8E487
NCBI Ref SeqWP_000728848.1
UniProtKB Sequence>tr|Q8E487|Q8E487_STRA3 Uncharacterized protein OS=Streptococcus agalactiae serotype III (strain NEM316) GN=gbs1515 PE=4 SV=1 MKKKNLLQESINKRLSEERYQIPKEKREKKRFDMQLILIISILIGLIMSIIGIIRFFLTY SS
EMBL CDSCAD47174.1
Sequence length62 AA
Subcellular LocationMembrane (Integral component of membrane)
String211110.gbs1515. 
Glycosyltransferase Information
Glycosylation TypeO- (Ser/Thr) linked 
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential
Donor TypeGlcNAc and sialic acid
Donor SpecificityNucleotide activated sugars
Accessory GT IDProGT33.1,ProGT33.2,ProGT33.3,ProGT33.4,ProGT33.5,ProGT33.6
Glycan Information
Method of Glycan IndentificationLC-MS/MS (ETD, CID and HCD)
Experimental_strategiesIn vivo 
Acceptor Subtrate Information
Acceptor Substrate name Srr1
ProGPdb ID ProGP316
Litrature
Year Of Validation2009 
Reference Mistou, M.Y., Dramsi, S., Brega, S., Poyart, C. and Trieu-Cuot, P., 2009. Molecular dissection of the secA2 locus of group B Streptococcus reveals that glycosylation of the Srr1 LPXTG protein is required for full virulence. Journal of bacteriology, 191(13), pp.4195-4206.

Corresponding AuthorInstitut Pasteur, Biological Unit of Gram-Positive Pathogenic Bacteria, URA CNRS 2172, Paris Cedex 15, France.
Reference Chaze, T., Guillot, A., Valot, B., Langella, O., Chamot-Rooke, J., Di Guilmi, A.M., Trieu-Cuot, P., Dramsi, S. and Mistou, M.Y., 2014. O-Glycosylation of the N-terminal region of the serine-rich adhesin Srr1 of Streptococcus agalactiae explored by mass spectrometry. Molecular & Cellular Proteomics, 13(9), pp.2168-2182.

Corresponding AuthorINRA, MICALIS UMR-1319, 78352 Jouy-en-Josas cedex, France