Latest update: September 24, 2018


ProGT29.2 (Gly)

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ProGT ID ProGT29.2 (Gly)
ProGT Pathway
Organism Information
Organism NameStreptococcus parasanguinis FW213
Domain Bacteria
PhylumFirmicutes
ClassificationFamily: Streptococcaceae
Order: Lactobacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI)1114965
Genome Information
Gene BankCP003122.1
EMBLCP003122.1
Gene Information
Gene NameGly 
Protein information
Protein NameGly 
UniProtKB/ SwissProt IDI1ZPA3
NCBI Ref SeqAFJ26877.1
UniProtKB Sequence>tr|I1ZPA3|I1ZPA3_STRPA Putative glycosyltransferase (Gly) OS=Streptococcus parasanguinis FW213 GN=gly PE=4 SV=1 MIRRVMEKISVIIPAYNAEKYLEQCVESVRTQIYNNIEIIIVNDGSTDRTAEIIERLKEK DSRIRTLHKRINEGIGATRNSALELVTGQYILFLDSDDWIDPNHISDLYNLLVRTDSDVS IANFTRYIESDNRYEIHITDDDYYEQIFTPQEWFTYQYGKPHNLSLCFTVPWGKLYKRSL FDNILYYTGPFGEDDRTTWKLYLVADKIAYMHRSTMVYRVNGESLTQTTERSEVFSVEPV LERLALLSMLGFDLKNEIAAFDWRANLVKNISLANGNVELYKELQFQLNMIEKYRKN
EMBL CDSAFJ26877.1
Sequence length297 AA
Glycosylation Information
CAZY FamilyGT2
EC Number (BRENDA)2.4.99.18
Sugar Donor Specificity UDP-Glucose or UDP-Galactose 
Experimental ValidationIn vivo and In vitro
Donor Specificity UDP-Glucose or UDP-Galactose
Additional Information1) Gly is a glucosyltransferase mediating the final step of Fap1 glycosylation.
2) Gly can transfer Glucose and Galactose, in vitro on Fap1 but it has higher activity toward transferring glucose.  
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