ProGP410 (DsbA)

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ProGP ID ProGP410 (DsbA)
Validation Status Characterized
Organism Information
Organism NameFrancisella tularensis ssp. tularensis strain SCHU S4 substr. FSC237 (type A strain)
Domain Bacteria
Classification Phylum : Proteobacteria
Class : Gammaproteobacteria
Orders : Thiotrichales
Family : Francisellaceae
Genus : Francisella
Species : tularensis
Subspecies : tularensis
Strain : SCHU S4
Taxonomic ID (NCBI) 1341660
Genome Information
GenBank AJ749949.2
EMBL AJ749949.2
Organism Additional Information Non-motile, 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 WP_003021256.1
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
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
Protein Glycosylation linked (PGL) gene(s)
Characterized Accessory Gene(s)FTT_0791 and FTT_0798
Additional CommentFTT0791 and FTT0798 genes are involved in DsbA glycosylation. FTT0791 shows sequence homology with UDP-galactose-4-epimerase (GalE) from other bacteria. GalE catalyzes interconversion of UDP-galactose to UDP-glucose in many bacteria, therefore involvement of the FTT0791 gene in protein glycosylation suggests that the hexasaccharide moieties are likely to be galactose.
Literature
Year of Identification2011
Year of Identification Month Wise2011.1
Year of Validation 2011
ReferenceThomas, R.M., Twine, S.M., Fulton, K.M., Tessier, L., Kilmury, S.L., Ding, W., Harmer, N., Michell, S.L., Oyston, P.C., Titball, R.W. and Prior, J.L., 2011. Glycosylation of DsbA in Francisella tularensis subsp. tularensis. Journal of bacteriology, 193(19), pp.5498-5509.
Corresponding Author Richard W. Titball
ContactCollege of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, United Kingdom