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ProGT33 (GtfA)

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ProGT ID ProGT33 (GtfA)
Organism Information
Organism NameStreptococcus agalactiae serotype III (strain NEM316)
Clinical ImplicationPathogenic
DomainBacteria
PhylumFirmicutes
ClassificationFamily: Streptococcaceae
Order: Lactobacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
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 TypeNucleotide activated sugars
Donor SpecificityGlcNAc and sialic acid
Accessory GT IDProGT33.1ProGT33.2ProGT33.3ProGT33.4ProGT33.5ProGT33.6
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., & 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), 4195-4206.

Authors Mistou, M. Y., Dramsi, S., Brega, S., Poyart, C., & Trieu-Cuot, P.
Research groupsInstitut Pasteur, Biological Unit of Gram-Positive Pathogenic Bacteria, URA CNRS 2172, Paris Cedex 15, France.
Corresponding Author Trieu-Cuot, P.
ContactsInstitut 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. & 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, mcp-M114.

Authors Chaze, T., Guillot, A., Valot, B., Langella, O., Chamot-Rooke, J., Di Guilmi, A.M., Trieu-Cuot, P., Dramsi, S. & Mistou, M. Y.
Research groups1 INRA MICALIS UMR 1319, 78352 Jouy-en-Josas cedex, France; AgroParisTech, MICALIS UMR 1319, 78352 Jouy-en-Josas cedex, France; Shepherd Institute, Mass Spectrometry and Proteomics Structural Unit, 28 rue du Dr. Roux, 75015 Paris, France 2 INRA, PAPPSO, MICALIS UMR-1319, 78352 Jouy en Josas cedex, France 3INRA, PAPPSO, Plant Genetics UMR-320, Ferme du Moulon, 91190 Gif sur Yvette, France; 4 Shepherd Institute, Mass Spectrometry and Proteomics Structural Unit, 28 rue du Dr. Roux, 75015 Paris, France; CNRS UMR 3528, Pasteur Institute, 28 rue du Dr. Roux, 75015 Paris, Francee 5 CEA, Institute of Structural Biology Jean-Pierre Ebel, F-38027 Grenoble, France 6 Institut Pasteur Bacteria Biology of Pathogenic Gram +, 28, rue du Dr Roux, 75015 Paris, France; Centre National Center for Scientific Research, CNRS ERL3526, Paris, France 7 INRA MICALIS UMR 1319, 78352 Jouy-en-Josas cedex, France
Corresponding Author Mistou, M. Y.
ContactsINRA, MICALIS UMR-1319, 78352 Jouy-en-Josas cedex, France