ProGP107

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

ProGP ID ProGP107
Validation Status Characterized
Organism Information
Organism NamePseudomonas aeruginosa 1244
Domain Bacteria
Classification Family: Pseudomonadaceae
Order: Pseudomonadales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 287
Genome Sequence(s)
GenBank X83916
EMBL X83916
Organism Additional Information This Gram-negative opportunistic pathogen is responsible for nosocomial pneumonia. It possesses a multitude of virulence factors including type IV pili that mediate adhesion to host cells. It is also the major cause of mortality among cystic fibrosis (CF) patients.
Gene Information
Gene NamepilA
Protein Information
Protein NameFimbrial protein (pilin); (group I T4P)
UniProtKB/SwissProt ID P18774
NCBI RefSeq WP_058150672.1
EMBL-CDSCAA58768.1
UniProtKB Sequence >sp|P18774|FM12_PSEAE Fimbrial protein OS=Pseudomonas aeruginosa GN=pilA PE=1 SV=1 MKAQKGFTLIELMIVVAIIGILAAIAIPQYQDYTARTQVTRAVSEVSALKTAAESAILEG KEIVSSATPKDTQYDIGFTESTLLDGSGKSQIQVTDNQDGTVELVATLGKSSGSAIKGAV ITVSRKNDGVWNCKITKTPTAWKPNYAPANCPKS
Sequence length 154 AA
Subcellular LocationSurface
Function Structural unit of the pili which have a role in pathogenesis. They are required for colonization through adhesion and and mediating surface translocation (twitching).
Glycosylation Status
Glycosylation Type O- (Ser) linked
Experimentally Validated Glycosite(s) in Full Length Protein(Propeptide: 1-6) S154 (C-terminal residue)
Experimentally Validated Glycosite(s ) in Mature ProteinS148 (C-terminal residue)
Glycosite(s) Annotated Protein Sequence >sp|P18774|FM12_PSEAE Fimbrial protein OS=Pseudomonas aeruginosa GN=pilA PE=1 SV=1 MKAQKGFTLIELMIVVAIIGILAAIAIPQYQDYTARTQVTRAVSEVSALKTAAESAILEG KEIVSSATPKDTQYDIGFTESTLLDGSGKSQIQVTDNQDGTVELVATLGKSSGSAIKGAV ITVSRKNDGVWNCKITKTPTAWKPNYAPANCPKS*(154)
Sequence Around Glycosites (21 AA) PNYAPANCPKS
Technique(s) used for Glycosylation DetectionDIG glycan detection (labeling with digoxigenin-succinyl-epsilon-amidocaproic acid hydrazide and anti-DIG antibody after periodate oxidation)
Technique(s) used for Glycosylated Residue(s) Detection N-terminal sequencing and site-directed mutagenesis
Protein Glycosylation- Implication Pilin glycosylation may function to protect the pilus against attack from proteolytic enzymes present as part of the host defense or as produced by P. aeruginosa itself. Presence of glycans, e.g., 5NβOHC47NfmPse on pilin fibrous structure would introduce a negative charge that would lower the pilus isoelectric point, influence solubility, and likely increase ionic interaction among pili and between the pili and extracellular structures therby influencing pilus-dependent functions such as twitching motility and biofilm formation, processes that are important in pathogenesis as well.
Glycan Information
Glycan Annotation Linkages: β-D-FucNAc-Ser.
A 666.5 Da trisaccharide containing pseudaminic acid, xylose, and N-acetylfucosamine [α-5NβOHC4 7NFmPse-(2→4)-β-Xyl-(1→3)-β-D-FucNAc-(1→3)-β-Ser].
Protein glycan molar ratio is 1:1.
It is structurally identical to the O-antigen repeating unit of P. aeruginosa serotype O7 LPS. This fact together with mutation studies suggest that the metabolic source of the pilin glycan is the O-antigen biosynthetic pathway. The pilin glycan differs from the O-antigen only in that the FucNAc residue is not O-acetylated.
BCSDB ID1697
Technique(s) used for Glycan Identification The gradient NMR spectrum, tandem MS/MS analysis, and methylation analysis provided information on linkage and the sequence of oligosaccharide components. Xylosyl linkage was determined by GLC-MS analysis of partially methylated alditol acetate.
Protein Glycosylation linked (PGL) gene(s)
OST Gene NamePilO (TfpO)
OST ProGT IDProGT1
Characterized Accessory Gene(s)WbpM, WbpL are encoded in the O-antigen biosynthesis cluster. WbpM is a UDP-GlcNAc C6 dehydratase/C4 reductase involved in the UDP-FucNAc biosynthesis. WbpL is a glycosyltransferase that transfers FucNAc from UDP-FucNAc to undecaprenol phosphate.
Accessory Gene(s)Progt IDProGT1.1,ProGT1.2
Additional CommentO-antigen sugars are not sequentially added to the pilin. wbpM and wbpL are essential for the initial steps of O-antigen biosynthesis.
5-N-3 hydroxybutyryl-7-N-formylpseudaminic acid is a part of a trisaccharide modification on P. aeruginosa pilin. It is the second example of glycoprotein with pseudaminic acid containing glycan apart from Campylobacter flagellin protein.
The substrate recognition features required for catalysis by PilO enzyme have been shown to be present in the first (reducing) sugar, β-D-FucNAc.
Literature
Year of Identification1995
Year of Identification Month Wise1995.05
Year of Validation 2002
ReferenceHorzempa, J., Dean, C.R., Goldberg, J.B. and Castric, P. (2006) Pseudomonas aeruginosa 1244 pilin glycosylation: glycan substrate recognition. J Bacteriol, 188, 4244-4252. [PubMed: 16740931]
AuthorHorzempa, J., Dean, C.R., Goldberg, J.B. and Castric, P.
Research GroupDepartment of Biological Sciences, Duquesne University, 600 Forbes Ave., Pittsburgh, PA 15282, USA.
Corresponding Author Castric, P.
ContactDepartment of Biological Sciences, Duquesne University, 600 Forbes Ave., Pittsburgh, PA 15282, USA.
Reference Smedley, J.G., 3rd, Jewell, E., Roguskie, J., Horzempa, J., Syboldt, A., Stolz, D.B. and Castric, P. (2005) Influence of pilin glycosylation on Pseudomonas aeruginosa 1244 pilus function. Infect Immun, 73, 7922-7931. [PubMed: 16299283]
Author Smedley, J.G., 3rd, Jewell, E., Roguskie, J., Horzempa, J., Syboldt, A., Stolz, D.B. Castric, P.
Research GroupDepartment of Biological Sciences, Duquesne University, Pittsburgh, PA 15282, USA.
Corresponding Author Castric, P.
ContactDepartment of Biological Sciences, Duquesne University, Pittsburgh, PA 15282, USA.
Reference Smedley, J.G., 3rd, Jewell, E., Roguskie, J., Horzempa, J., Syboldt, A., Stolz, D.B. and Castric, P. (2005) Influence of pilin glycosylation on Pseudomonas aeruginosa 1244 pilus function. Infect Immun, 73, 7922-7931. [PubMed: 16299283]
Author Smedley, J.G., 3rd, Jewell, E., Roguskie, J., Horzempa, J., Syboldt, A., Stolz, D.B. Castric, P.
Research GroupDepartment of Biological Sciences, Duquesne University, Pittsburgh, PA 15282, USA
Corresponding Author Castric, P.
ContactDepartment of Biological Sciences, Duquesne University, Pittsburgh, PA 15282, USA
Reference Comer, J.E., Marshall, M.A., Blanch, V.J., Deal, C.D. and Castric, P. (2002) Identification of the Pseudomonas aeruginosa 1244 pilin glycosylation site. Infect Immun, 70, 2837-2845. [PubMed: 12010970]
Author Comer, J.E., Marshall, M.A., Blanch, V.J., Deal, C.D. Castric, P.
Research GroupDepartment of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA.
Corresponding Author Castric, P.
ContactDepartment of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA.
Reference DiGiandomenico, A., Matewish, M.J., Bisaillon, A., Stehle, J.R., Lam, J.S. and Castric, P. (2002) Glycosylation of Pseudomonas aeruginosa 1244 pilin: glycan substrate specificity. Mol Microbiol, 46, 519-530. [PubMed: 12406226]
Author DiGiandomenico, A., Matewish, M.J., Bisaillon, A., Stehle, J.R., Lam, J.S. and Castric, P.
Research GroupDepartment of Biological Sciences, Duquesne University, Pittsburg, PA 15282, USA.
Corresponding Author Castric, P.
ContactDepartment of Biological Sciences, Duquesne University, Pittsburg, PA 15282, USA.
Reference Castric, P., Cassels, F.J. and Carlson, R.W. (2001) Structural characterization of the Pseudomonas aeruginosa 1244 pilin glycan. J Biol Chem, 276, 26479-26485. [PubMed: 11342554]
Author Castric, P., Cassels, F.J. Carlson, R.W.
Research GroupDepartment of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA.
Corresponding Author Carlson, R.W.
ContactDepartment of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA.
Reference Castric, P. (1995) pilO, a gene required for glycosylation of Pseudomonas aeruginosa 1244 pilin. Microbiology, 141 ( Pt 5), 1247-1254. [PubMed: 7773418]
Author Castric, P
Research GroupDepartment of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA.
Corresponding Author Castric, P
ContactDepartment of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA.