ProGP494 (FliC (Flagellin))
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| ProGP ID | ProGP494 (FliC (Flagellin)) |
| Validation Status | Uncharacterized |
| Organism Information | |
| Organism Name | Burkholderia cenocepacia K56-2 |
| Domain | Bacteria |
| Classification | Family: Burkholderiaceae Order: Burkholderiales Class: Betaproteobacteria Division or phylum: "Proteobacteria" |
| Taxonomic ID (NCBI) | 985075 |
| Genome Information | |
| GenBank | NZ_LAUA01000000 |
| EMBL | LAUA01000000 |
| Organism Additional Information | Burkholderia cenocepacia causes opportunistic infections in plants, insects, animals and humans. It acts as a health threat to cystic fibrosis patients, causing lethal necrotizing pneumonia in some cases. |
| Gene Information | |
| Gene Name | FliC (BCAL0114) |
| NCBI Gene ID | KC763156 |
| GenBank Gene Sequence | KC763156.1 |
| Protein Information | |
| Protein Name | FliC (Flagellin) |
| UniProtKB/SwissProt ID | M9YNZ2 |
| NCBI RefSeq | AGK24641.1 |
| EMBL-CDS | AGK24641.1 |
| UniProtKB Sequence | >tr|M9YNZ2|M9YNZ2_9BURK Flagellin OS=Burkholderia cenocepacia GN=fliC PE=3 SV=1 MLGINSNINSLVAQQNLNGSQNALSQAITRLSSGKRINSAADDAAGLAISTRMQTQINGL NQGVSNANDGVSMIQTASSALSSLTNSLQRIRQLAVQASTGTMSTTDQAALQQEVSQQIQ EVNRIASQTTYNGTNILDGSAGIVSFQVGANVGQTISLDLSQSMSAAKIGGGLVQKGQTV GTVTGLSLDNNGAYTGSGATITAINVLSDGKGGYTFTDQNGGAISQTVAQSVFGANATTG TGTAVGNLTLQSGATGAGTSAAQQTAITNAIAQINAVNKPATVSNLDISTVSGANVAMVS IDNALQTVNNVQAALGAAQNRFTAIATSQQAESTDLSSAQSQITDANFAQETANMSKNQV LQQAGISVLAQANSLPQQVLKLLQ |
| Sequence length | 384 AA |
| Subcellular Location | Secreted Flaggellin |
| Function | Motility |
| Glycosylation Status | |
| Glycosylation Type | O- (Ser/Thr) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | 10 glycosites identified each with 231 Da modification |
| Technique(s) used for Glycosylation Detection | Digestion with Trypsin, Chymotrypsin, AspN and mixture of AspN and trypsin and then MS and MSMS |
| Protein Glycosylation- Implication | The O-antigen cluster gene rmlB is required for bacterial viability. Flagellin glycan was shown to impair the inflammatory response of epithelial cells. The glycosylation was suggested to help the infecting bacteria in immune evasion by reducing the flagellin recognition through host TLR5. |
| Glycan Information | |
| Glycan Annotation | 4,6-dideoxy-4-(3-hydroxybutanoylamino)-D-glucose. Protein is glycosylated on at least ten different sites. |
| Technique(s) used for Glycan Identification | GC/MS ( Beta elimination) |
| Protein Glycosylation linked (PGL) gene(s) | |
| OST Gene Name | FlmQ |
| OST ProGT ID | ProGT74 (FilmQ) |
| Literature | |
| Reference | Hanuszkiewicz, A., Pittock, P., Humphries, F., Moll, H., Rosales, A.R., Molinaro, A., Moynagh, P.N., Lajoie, G.A. and Valvano, M.A., 2014. Identification of the flagellin glycosylation system in Burkholderia cenocepacia and the contribution of glycosylated flagellin to evasion of human innate immune responses. Journal of Biological Chemistry, 289(27), pp.19231-19244. |
| Corresponding Author | Valvano MA |
| Contact | From the Centre for Infection and Immunity, School of Medicine, Dentistry and Biomedical Sciences, Queen's University, Belfast BT9 7AE, Ireland, United Kingdom, the Department of Microbiology and Immunology, University of Western Ontario, London, Ontario N6A 5C1, Canada, |
| Reference | Hanuszkiewicz A, Pittock P, Humphries F, Moll H, Rosales AR, Molinaro A, Moynagh PN, Lajoie GA, Valvano MA. (2014) Identification of the flagellin glycosylation system in Burkholderia cenocepacia and the contribution of glycosylated flagellin to evasion of human innate immune responses. J Biol Chem. 289, 19231-44. [PMID: 24841205 ] |
| Author | Hanuszkiewicz A, Pittock P, Humphries F, Moll H, Rosales AR, Molinaro A, Moynagh PN, Lajoie GA, Valvano MA. |
| Research Group | 1 Centre for Infection and Immunity, School of Medicine, Dentistry and Biomedical Sciences, Queens University, Belfast BT9 7AE, Ireland, United Kingdom. 2 the Don Rix Protein Identification Facility, Department of Biochemistry, University of Western Ontario, London, Ontario N6A 5C1, Canada. 3 the Institute of Immunology, Department of Biology, National University of Ireland at Maynooth, Maynooth, County Kildare, Ireland. 4 the Bioanalytical Chemistry, Research Centre Borstel, 23845 Borstel, Germany. 5 the Department of Microbiology and Immunology, University of Western Ontario, London, Ontario N6A 5C1, Canada, and. 6 the Dipartimento di Scienze Chimiche, Università di Napoli, Federico II, 80134 Naples, Italy. 7 From the Centre for Infection and Immunity, School of Medicine, Dentistry and Biomedical Sciences, Queens University, Belfast BT9 7AE, Ireland, United Kingdom, the Institute of Immunology, Department of Biology, National University of Ireland at Maynooth, Maynooth, County Kildare, Ireland. 8 From the Centre for Infection and Immunity, School of Medicine, Dentistry and Biomedical Sciences, Queens University, Belfast BT9 7AE, Ireland, United Kingdom, the Department of Microbiology and Immunology, University of Western Ontario, London, Ontario N6A 5C1, Canada, |
| Corresponding Author | Valvano MA |
| Contact | Centre for Infection and Immunity, School of Medicine, Dentistry and Biomedical Sciences, Queens University, Belfast BT9 7AE, Ireland, United Kingdom, the Department of Microbiology and Immunology, University of Western Ontario, London, Ontario N6A 5C1, Canada, |