ProGP343 (PilA (FTH_0384))

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ProGP ID ProGP343 (PilA (FTH_0384))
Validation Status Characterized
Organism Information
Organism NameFrancisella tularensis ssp. holarctica strain FSC200
Domain Bacteria
Classification Family: Francisellaceae
Order:Thiotrichales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 351581
Genome Information
GenBank CP003862.1
EMBL CP003862.1
Gene Information
Gene NamePilA (FTH_0384)
GenBank Gene Sequence NC_008369.1
Protein Information
Protein NamePilA (FTH_0384)
UniProtKB/SwissProt ID A0SP58
NCBI RefSeq WP_011648587.1
EMBL-CDSAAX14621.1
UniProtKB Sequence >tr|A0SP58|A0SP58_FRATU PilE1 OS=Francisella tularensis subsp. holarctica GN=pilA PE=3 SV=1 MKKKMQKGFSLVELMVVIAIIAILAAVAIPMYSNYTTRAQLGSDLSALGGAKAIVAEKIA NNNGDASQVTILQANAAANGLPSGASVAAGTISYPSTVSGATIQLAPTVSSGAITWTCNI SGVSASQVPSNCNAI
Sequence length 135 AA
Subcellular LocationMembrane
Function Type IV pili fiber building block protein
Protein Structure
Protein Additional InformationThis protein shares 52.5% similarity with pilE1-encoded pilin (FMM1_NEIGO) of N. gonorrheae, which is modified with Gal 1-3GlcNAc at Ser70.
Glycosylation Status
Glycosylation Type O- (Ser/Thr) linked
Experimentally Validated Glycosite(s) in Full Length ProteinOne of either S103 or S102
Glycosite(s) Annotated Protein Sequence >tr|A0SP58|A0SP58_FRATU PilE1 OS=Francisella tularensis subsp. holarctica GN=pilA PE=3 SV=1 MKKKMQKGFSLVELMVVIAIIAILAAVAIPMYSNYTTRAQLGSDLSALGGAKAIVAEKIA NNNGDASQVTILQANAAANGLPSGASVAAGTISYPSTVSGATIQLAPTVS*(102)S*(103)GAITWTCNI SGVSASQVPSNCNAI
Sequence Around Glycosites (21 AA) GATIQLAPTVSSGAITWTCNI
ATIQLAPTVSSGAITWTCNIS
Technique(s) used for Glycosylation DetectionHydrazide labeling and lectin affinity chromatography.
Technique(s) used for Glycosylated Residue(s) Detection MSMS (Ion trap with electron transfer dissociation (ETD))
Protein Glycosylation- Implication Pilin glycosylation has been shown to play a role in host-cell adhesion and virulence.
Glycan Information
Glycan Annotation Pentasaccharide (HexNAc-Hex-Hex-HexNAc-HexNAc) is linked through its terminal HexNAc residue to a 162.111-Da moiety via a phosphate bridge.
Technique(s) used for Glycan Identification MS (ion trap with tandemMS CID and ETD)
Protein Glycosylation linked (PGL) gene(s)
OST Gene NamePglA
OST ProGT IDProGT50 (PglA)
Literature
ReferenceBalonova, L., Hernychova, L., Mann, B.F., Link, M., Bilkova, Z., Novotny, M.V. and Stulik, J., 2010. Multimethodological approach to identification of glycoproteins from the proteome of Francisella tularensis, an intracellular microorganism. Journal of proteome research, 9(4), pp.1995-2005.
Corresponding Author Lenka Hernychova
ContactInstitute of Molecular Pathology, Faculty of Military Health Sciences, University of Defence, Hradec Kralove, Czech Republic
ReferenceEgge-Jacobsen, W., Salomonsson, E.N., Aas, F.E., Forslund, A.L., Winther-Larsen, H.C., Maier, J., Macellaro, A., Kuoppa, K., Oyston, P.C., Titball, R.W. and Thomas, R.M., 2011. O-linked glycosylation of the PilA pilin protein of Francisella tularensis: identification of the endogenous protein-targeting oligosaccharyltransferase and characterization of the native oligosaccharide. Journal of bacteriology, 193(19), pp.5487-5497.
Corresponding Author Wolfgang Egge-Jacobsen
Michael Koomey
Contacta.Department of Molecular Biosciences and b.Center for Molecular Biology and Neuroscience, University of Oslo, Oslo 0316, Norway
ReferenceBalonova, L., Mann, B.F., Cerveny, L., Alley, W.R., Chovancova, E., Forslund, A.L., Salomonsson, E.N., Forsberg, Å., Damborsky, J., Novotny, M.V. and Hernychova, L., 2012. Characterization of protein glycosylation in Francisella tularensis subsp. holarctica: identification of a novel glycosylated lipoprotein required for virulence. Molecular & Cellular Proteomics, 11(7), pp.M111-015016.
Corresponding Author Lenka Hernychova
ContactInstitute of Molecular Pathology, Faculty of Military Health Sciences, University of Defence, Hradec Kralove, Czech Republic
ReferenceBalonova L, Hernychova L, Mann BF, Link M, Bilkova Z, Novotny MV, Stulik J. (2010) Multimethodological approach to identification of glycoproteins from the proteome of Francisella tularensis, an intracellular microorganism. J Proteome Res., 9, 1995-2005. [PMID: 20175567]
AuthorBalonova L, Hernychova L, Mann BF, Link M, Bilkova Z, Novotny MV, Stulik J.
Research GroupInstitute of Molecular Pathology, Faculty of Military Health Sciences, University of Defence, Hradec Kralove, Czech Republic
Corresponding Author Stulik J.
ContactInstitute of Molecular Pathology, Faculty of Military Health Sciences, University of Defence, Hradec Kralove, Czech Republic
ReferenceEgge-Jacobsen W, Salomonsson EN, Aas FE, Forslund AL, Winther-Larsen HC, Maier J, Macellaro A, Kuoppa K, Oyston PC, Titball RW, Thomas RM, Forsberg Å, Prior JL, Koomey M. (2011) O-linked glycosylation of the PilA pilin protein of Francisella tularensis: identification of the endogenous protein-targeting oligosaccharyltransferase and characterization of the native oligosaccharide. J Bacteriol., 193, 5487-97. [PMID: 21804002]
AuthorEgge-Jacobsen W, Salomonsson EN, Aas FE, Forslund AL, Winther-Larsen HC, Maier J, Macellaro A, Kuoppa K, Oyston PC, Titball RW, Thomas RM, Forsberg Å, Prior JL, Koomey M
Research GroupDepartment of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway
Corresponding Author Koomey M
ContactDepartment of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway
ReferenceBalonova L, Mann BF, Cerveny L, Alley WR Jr, Chovancova E, Forslund AL, Salomonsson EN, Forsberg A, Damborsky J, Novotny MV, Hernychova L, Stulik J. (2012) Characterization of protein glycosylation in Francisella tularensis subsp. holarctica: identification of a novel glycosylated lipoprotein required for virulence. Mol Cell Proteomics, 11(7), M111. [PMID: 22361235]
Author Lucie Balonova, Benjamin F. Mann, Lukas Cerveny, William R. Alley, Jr.,Eva Chovancova , Anna-Lena Forslund, Emelie N. Salomonsson, Åke Forsberg, Jiri Damborsky , Milos V. Novotny, Lenka Hernychova, and Jiri Stulik.
Research GroupInstitute of Molecular Pathology, Faculty of Military Health Sciences, University of Defence, 500 01 Hradec Kralove, Czech Republic.
Corresponding Author Jiri Stulik.
ContactInstitute of Molecular Pathology, Faculty of Military Health Sciences, University of Defence, 500 01 Hradec Kralove, Czech Republic.