ProGP343 (PilA (FTH_0384))

Home -> ProGPdb -> Search ProGP -> Display data

ProGP ID ProGP343 (PilA (FTH_0384))
Validation Status Characterized
Organism Information
Organism NameFrancisella tularensis ssp. holarctica strain FSC200
Domain Bacteria
Classification Phylum : Proteobacteria
Class : Gammaproteobacteria
Orders : Thiotrichales
Family : Francisellaceae
Genus : Francisella
Species : tularensis
Subspecies : holarctica
Strain : FSC 200
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
Literature
Year of Identification2010
Year of Identification Month Wise2010.04
Year of Validation 2011
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