Latest update: September 24, 2018


ProGT29.1 (GalT2)

Home -> ProGTdb -> Search ProGT_Accessory -> Display data

ProGT ID ProGT29.1 (GalT2)
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 NamegalT2 
Protein information
Protein NameGalT2 
UniProtKB/ SwissProt IDI1ZPA0
NCBI Ref SeqWP_014713997.1
UniProtKB Sequence>tr|I1ZPA0|I1ZPA0_STRPA Putative glycosyltransferase (GalT2) OS=Streptococcus parasanguinis FW213 GN=galT2 PE=4 SV=1 MEKISVIVPIYNAGEYLRPCLDSIVNQSYSNLEIILINDGSTDTSAAVCEEYLHRDSRIR IVQKKLGGSGVGAARNSALPLVTGDFILFVDNDDWLELNHIEILYQDLKETGSDIAVTNF TEFFEERQSFAFHVDLSDPYLEVYTPQEWFRKQYDGRLSFSQCFTVPWGKLYKAELFQDI VYPEEEKVEDDLTTWKVYLMADRISYRNLGLYYHRKRSTSVTRVVEMEHVFPIKSIEERV TILSLIGFEISNELRAYKWRLQKHKESYLSRGDVYNYKKCLQKIKIIEKWQAK
EMBL CDSAFJ26874.1
Sequence length293 AA
Glycosylation Information
CAZY FamilyGT2
EC Number (BRENDA)2.4.1.-
Experimental ValidationIn vivo
Additional Information1) GalT2 is the first rhamnosyltransferase involved in the glycosylation of a bacterial adhesin.  
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