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 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 NamepilA (FTT_0890c)
GenBank Gene Sequence AJ749949.2
Protein Information
Protein NamePilA (Pilin)
UniProtKB/SwissProt ID Q5NGF5
NCBI RefSeq CAG45523.1
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
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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
Additional CommentPglA is necesarry for PilA glycosylation in Francisella tularensis and sufficient for PilA glycosylation in Escherichia coli. Coexpression of F. tularensis PilA and PglA F or F. tularensis PilA and N. gonorrhoeae OST PilO along with N. gonorrhoeae core pgl locus in E.coli was sufficient to glycosylate F. tularensis PilA. F. tularensis PilA also gets O-glycosylated when expressed in N. gonorrhoeae. F. tularensis PilA has also been identiifed to be associated with phosphoglycans. The similar phenomenon of O-linked phosphoglycan has been previously observed in Clostridium difficile and Pseudomonas aeruginosa, where the phosphates have been suggested to bridge sugars to a methylated form of aspartic acid and an unknown terminal modification, respectively.
Year of Identification2006
Year of Identification Month Wise2006.6.1
Year of Validation 2011
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
ContactDepartment of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway.
ReferenceForslund, A.L., Kuoppa, K., Svensson, K., Salomonsson, E., Johansson, A., Byström, M., Oyston, P.C., Michell, S.L., Titball, R.W., Noppa, L. and Frithz‐Lindsten, E., 2006. Direct repeat‐mediated deletion of a type IV pilin gene results in major virulence attenuation of Francisella tularensis. Molecular microbiology, 59(6), pp.1818-1830.
Corresponding Author Åke Forsberg
ContactDepartment of Medical Countermeasures, Division of NBC-Defence, Swedish Defence Research Agency, Umea ,2.Department of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden.
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