ProGP410 (DsbA)
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ProGP ID | ProGP410 (DsbA) |
Validation Status | Characterized |
Organism Information | |
Organism Name | Francisella 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 Name | DsbA (FTT_1103) |
NCBI Gene ID | 3191250 |
GenBank Gene Sequence | AJ749949.2 |
Protein Information | |
Protein Name | DsbA |
UniProtKB/SwissProt ID | Q5NFW3 |
NCBI RefSeq | WP_003021256.1 |
EMBL-CDS | AJI68392.1 |
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 Location | Periplasm |
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 Protein | S355 |
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 Detection | 2D-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 Comment | FTT0791 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 Identification | 2011 |
Year of Identification Month Wise | 2011.1 |
Year of Validation | 2011 |
Reference | Thomas, 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 |
Contact | College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, United Kingdom |