ProGP1215 (BCAL0525 (FliF))
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| ProGP ID | ProGP1215 (BCAL0525 (FliF)) |
| Validation Status | Uncharacterized |
| Organism Information | |
| Organism Name | Burkholderia cenocepacia |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : Betaproteobacteria Orders : Burkholderiales Family : Burkholderiaceae Genus : Burkholderia Species : cenocepacia |
| Taxonomic ID (NCBI) | 95486 |
| Genome Information | |
| GenBank | AM747720.1 |
| EMBL | AM747720 |
| Organism Additional Information | Burkholderia cenocepacia is a species of Gram-negative bacteria that is common in the environment, can form a biofilm with itself, is resistant to many antibiotics[2] and may cause disease in plants |
| Gene Information | |
| Gene Name | BCAL0524 |
| Protein Information | |
| Protein Name | BCAL0525 (FliF) |
| UniProtKB/SwissProt ID | B4E816 |
| NCBI RefSeq | CAR50835 |
| UniProtKB Sequence | >CAR50835.1 flagellar M-ring protein FliF [Burkholderia cenocepacia J2315] MDSQANSLINPDARAGLSPAPGAAAAAALPGAGGAGADFGLGGFAERIPGISRMKGNPKLPFVIAVAFAIAAITALVLWSRAPDYRVLYSNLSDRDGGAIIAALQQANVPYKFADAGGAILVPSNQVHETRLKLAAMGLPKGGSVGFELMDNQKFGISQFAEQINYQRALEGELQRTIESINAVRGARVHLAIPKPSVFVRDKEAPSASVFVDLYPGRVLDEGQVQAITRMVSSGVPDMPAKNVTIVDQDGNLLTQTASASGLDASQLKYVQQVEHNTQKRIDAILAPIFGAGNARSQVSADLDFSKIEQTSESYGPNGTPQQAAIRSQQTSSATELAQGGASGVPGALSNTPPQPASAPIVAGNGQNAPQTTPVSDRKDQTTNYELDKTIRHTEQPMGSVKRLSVAVVVNYQPVADAKGHVTMQPLPPAKLAQVEQLVKDAMGYDEKRGDSVNVVNSAFSTVSDPYADLPWWRQPDMIAMAKEAAKWLGIAAAAAALYFMFVRPAMRRAFPPPEPAAPALAAPEDAVALDGLPAPDKAAEEPDPLLLGFENEKNRYERNLDYARTIARQDPKIVATVVKNWVSDER |
| Function | flagellum-mediated motility and chemotaxis |
| Glycosylation Status | |
| Glycosylation Type | O- (Ser/Thr) linked |
| Experimentally Validated Glycosite(s ) in Mature Protein | >CAR50835.1 flagellar M-ring protein FliF [Burkholderia cenocepacia J2315] MDSQANSLINPDARAGLSPAPGAAAAAALPGAGGAGADFGLGGFAERIPGISRMKGNPKLPFVIAVAFAIAAITALVLWSRAPDYRVLYSNLSDRDGGAIIAALQQANVPYKFADAGGAILVPSNQVHETRLKLAAMGLPKGGSVGFELMDNQKFGISQFAEQINYQRALEGELQRTIESINAVRGARVHLAIPKPSVFVRDKEAPSASVFVDLYPGRVLDEGQVQAITRMVSSGVPDMPAKNVTIVDQDGNLLTQTASASGLDASQLKYVQQVEHNTQKRIDAILAPIFGAGNARSQVSADLDFSKIEQTSESYGPNGTPQQAAIRSQQTSSATELAQGGASGVPGALSNTPPQPASAPIVAGNGQNAPQTTPVSDRKDQTTNYELDKTIRHTEQPMGSVKRLSVAVVVNYQPVADAKGHVTMQPLPPAKLAQVEQLVKDAMGYDEKRGDSVNVVNSAFSTVSDPYADLPWWRQPDMIAMAKEAAKWLGIAAAAAALYFMFVRPAMRRAFPPPEPAAPALAAPEDAVALDGLPAPDKAAEEPDPLLLGFENEKNRYERNLDYARTIARQDPKIVATVVKNWVSDER |
| Literature | |
| Year of Identification | 2020 |
| Reference | Oppy, C.C., Jebeli, L., Kuba, M., Oates, C.V., Strugnell, R., Edgington-Mitchell, L.E., Valvano, M.A., Hartland, E.L., Newton, H.J. and Scott, N.E., 2019. Loss of O-linked protein glycosylation in Burkholderia cenocepacia impairs biofilm formation and siderophore activity and alters transcriptional regulators. Msphere, 4(6), pp.e00660-19. |
| Corresponding Author | Nichollas E Scott |
| Contact | Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Australia |