ProGP250 (PilA (Pilin))

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ProGP ID ProGP250 (PilA (Pilin))
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 Information
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 NamepilA (FTT_0890c)
GenBank Gene Sequence AJ749949.2
Protein Information
Protein NamePilA (Pilin)
UniProtKB/SwissProt ID Q5NGF5
NCBI RefSeq CAG45523.1
EMBL-CDSCAG45523.2
UniProtKB Sequence >tr|Q5NGF5|Q5NGF5_FRATT Type IV pili fiber building block protein OS=Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4) GN=FTT_0890c PE=3 SV=1 MKKKMQKGFSLVELMVVIAIIAILAAVAIPMYSNYTTRAQLGSDLSALGGAKATVAERIA NNNGDASQVTILQANAAANGLPSGASVAAGTISYPSTVSGATIQLAPTVSSGAITWTCNI SGVSASQVPSNCNAI
Sequence length 135 AA
Subcellular LocationMembrane
Function Cell adhesion
Protein Structure
Protein Additional Information Type IV pili fiber building block protein
Glycosylation Status
Glycosylation Type O- (Ser) linked
Experimentally Validated Glycosite(s) in Full Length ProteinOne of either S110 or S111
Glycosite(s) Annotated Protein Sequence >tr|Q5NGF5|Q5NGF5_FRATT Type IV pili fiber building block protein OS=Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4) GN=FTT_0890c PE=3 SV=1 MKKKMQKGFSLVELMVVIAIIAILAAVAIPMYSNYTTRAQLGSDLSALGGAKATVAERIA NNNGDASQVTILQANAAANGLPSGASVAAGTISYPSTVSGATIQLAPTVS*(110)S*(111)GAITWTCNI SGVSASQVPSNCNAI
Technique(s) used for Glycosylation DetectionImmunoblotting, Trypsin digestion and mass spectrometry (Ion trap with CID)
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). Orbitrap XL mass spectrometer using the higher-energy collisional fragmentation (HCD) mode suggests that pentasaccharide 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
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.
ReferenceForslund AL, Kuoppa K, Svensson K, Salomonsson E, Johansson A, Byström M, Oyston PC, Michell SL, Titball RW, Noppa L, Frithz-Lindsten E, Forsman M, Forsberg A. (2006) Direct repeat-mediated deletion of a type IV pilin gene results in major virulence attenuation of Francisella tularensis. Mol Microbiol., 59, 1818-30. [PMID: 16553886]
AuthorForslund AL, Kuoppa K, Svensson K, Salomonsson E, Johansson A, Byström M, Oyston PC, Michell SL, Titball RW, Noppa L, Frithz-Lindsten E, Forsman M, Forsberg A
Research GroupDepartment of Medical Countermeasures, Division of NBC-Defence, Swedish Defence Research Agency, Umea
Corresponding Author Forsberg A
ContactDepartment of Medical Countermeasures, Division of NBC-Defence, Swedish Defence Research Agency, Umea
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