ProGP414

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ProGP ID ProGP414
Validation Status Characterized
Organism Information
Organism NameFrancisella tularensis ssp. tularensis strain SCHU S4 substr. FSC237 (type A strain)
Domain Bacteria
Classification Family: Francisellaceae
Order: Thiotrichales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 1341660
Genome Sequence(s)
GenBank AJ749949.2
EMBL AJ749949.2
Organism Additional Information Nonmotile, nonsporulating, Gram-negative intracellular pathogen, causative agent of tularemia, affecting humans and rodents
Gene Information
Gene NameDsbA (FTT_1103)
NCBI Gene ID 3191250
GenBank Gene Sequence AJ749949.2
Protein Information
Protein NameDsbA
UniProtKB/SwissProt ID Q5NFW3
NCBI RefSeq YP_170079.1
EMBL-CDSAJI68392.1
UniProtKB Sequence >tr|Q5NFW3|Q5NFW3_FRATT Conserved hypothetical lipoprotein OS=Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4) GN=FTT_1103 PE=4 SV=1 MTKKKLLKALAVAAIATSLVACSDSSSNDKTLTTAVSSGSSVATTTVAAPADNTNVTANA SYIIGYGMGSSIATDKNIKTFNLNNDKVMAGFEDAINAKKPAIPLEDIANNMNTLRDKMQ QQMNQKAVTSFLSVQDGIYNSDLTPKSDIKNPDVVVYEFFDYQCMYCSKLAPEIEKIMKD NSDVQVVFAEFPIFGQKLPASEYAAEVSTAIYKLYGADAYVKYHNGIFATGEDEGSLKNA TVDNVAKQAGADMTKVNKAIQDDKIADHLKDMLKMGFGQLGIQGTPFLVIAPAKNATVAN TTIIGGYTTADGIQAAINKAKSTATTTSTSNNGQTDTKQAQNDIATVTAEAQATSGSTEQ LAQPR
Sequence length 365 AA
Subcellular LocationPeriplasm
Function Disulfide bond formation (through DsbA/DsbB system)
Protein Structure
Protein Additional Information A putative disulfide isomerase protein, in silico analysis suggests it to be a lipoprotein.
Glycosylation Status
Glycosylation Type O- (Ser/Thr) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS355
Glycosite(s) Annotated Protein Sequence >tr|Q5NFW3|Q5NFW3_FRATT Conserved hypothetical lipoprotein OS=Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4) GN=FTT_1103 PE=4 SV=1 MTKKKLLKALAVAAIATSLVACSDSSSNDKTLTTAVSSGSSVATTTVAAPADNTNVTANA SYIIGYGMGSSIATDKNIKTFNLNNDKVMAGFEDAINAKKPAIPLEDIANNMNTLRDKMQ QQMNQKAVTSFLSVQDGIYNSDLTPKSDIKNPDVVVYEFFDYQCMYCSKLAPEIEKIMKD NSDVQVVFAEFPIFGQKLPASEYAAEVSTAIYKLYGADAYVKYHNGIFATGEDEGSLKNA TVDNVAKQAGADMTKVNKAIQDDKIADHLKDMLKMGFGQLGIQGTPFLVIAPAKNATVAN TTIIGGYTTADGIQAAINKAKSTATTTSTSNNGQTDTKQAQNDIATVTAEAQATS*(355)GSTEQ LAQPR
Sequence Around Glycosites (21 AA) ATVTAEAQATSGSTEQLAQPR
Glycosite Sequence Logo
Technique(s) used for Glycosylation Detection2D-PAGE, Emerald Q glycostain, trypsin digestion and nLC-MS/MS
Technique(s) used for Glycosylated Residue(s) Detection Ion pairing normal-phase liquid chromatography (IP-NPLC) and nLC-MS/MS using Electron transfer dissociation (ETD)
Protein Glycosylation- Implication DsbA glycoprotein has been identified as an essential virulence factor of virulent type A F. tularensis.
Glycan Information
Glycan Annotation Hexasaccharide containing HexNAc-unknown sugar (X)-HexNAc-Hex-Hex-HexNAc (glycan mass 1156-Da )
Technique(s) used for Glycan Identification High-resolution multistage MS analyses
Literature
Year of Identification2011
Year of Identification Month Wise2011.1
Year of Validation 2011
ReferenceRebecca M. Thomas, Susan M. Twine, Kelly M. Fulton, Luc Tessier, Sara L. N. Kilmury, Wen Ding, Nicholas Harmer, Stephen L. Michell, Petra C. F. Oyston, Richard W. Titball and Joann L. Prior. (201Glycosylation of DsbA in Francisella tularensis subsp. tularensis.JOURNAL OF BACTERIOLOGY, Oct. 2011, p. 5498–5509
AuthorThomas RM, Twine SM, Fulton KM, Tessier L, Kilmury SL, Ding W, Harmer N, Michell SL, Oyston PC, Titball RW, Prior JL.
Research GroupDefence Science and Technology Laboratory, Porton Down, Salisbury SP4 0JQ, United Kingdom.
Corresponding Author Prior JL
ContactDefence Science and Technology Laboratory, Porton Down, Salisbury SP4 0JQ, United Kingdom.