ProGP107 (Fimbrial protein (pilin); (group I T4P))
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| ProGP ID | ProGP107 (Fimbrial protein (pilin); (group I T4P)) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Pseudomonas aeruginosa 1244 |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : Gammaproteobacteria Orders : Pseudomonadales Family : Pseudomonadaceae Genus : Pseudomonas Species : aeruginosa Strain : 1244 |
| Taxonomic ID (NCBI) | 287 |
| Genome Information | |
| 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 Name | pilA |
| Protein Information | |
| Protein Name | Fimbrial protein (pilin); (group I T4P) |
| UniProtKB/SwissProt ID | P18774 |
| NCBI RefSeq | WP_058150672.1 |
| EMBL-CDS | CAA58768.1 |
| 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 Location | Surface |
| 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 Protein | S148 (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 Detection | DIG 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 ID | 1697 |
| GlyTouCan | G44607ES |
| 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 Name | PilO (TfpO) |
| OST ProGT ID | ProGT1 |
| 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 ID | ProGT1.1,ProGT1.2 |
| Additional Comment | O-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 Identification | 1995 |
| Year of Identification Month Wise | 1995.05 |
| Year of Validation | 2002 |
| Reference | Horzempa, J., Dean, C.R., Goldberg, J.B. and Castric, P., 2006. Pseudomonas aeruginosa 1244 pilin glycosylation: glycan substrate recognition. Journal of bacteriology, 188(12), pp.4244-4252. |
| Corresponding Author | Peter Castric |
| Contact | Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA. castric@duq.edu |
| Reference | Smedley III, J.G., 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. Infection and immunity, 73(12), pp.7922-7931. |
| Corresponding Author | Peter Castric |
| Contact | Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA. castric@duq.edu |
| 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] |
| Corresponding Author | Peter Castric |
| Contact | Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA. castric@duq.edu |
| 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] |
| Corresponding Author | Peter Castric |
| Contact | Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA. castric@duq.edu |
| 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] |
| Corresponding Author | Peter Castric |
| Contact | Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA. castric@duq.edu |
| Reference | Castric, P. (1995) pilO, a gene required for glycosylation of Pseudomonas aeruginosa 1244 pilin. Microbiology, 141 ( Pt 5), 1247-1254. [PubMed: 7773418] |
| Corresponding Author | Peter Castric |
| Contact | Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA. castric@duq.edu |