ID M9YNZ2_9BURK Unreviewed; 384 AA. AC M9YNZ2; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 02-JUN-2021, entry version 41. DE RecName: Full=Flagellin {ECO:0000256|RuleBase:RU362073}; GN Name=fliC {ECO:0000313|EMBL:AGK24641.1}; OS Burkholderia cenocepacia. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=95486 {ECO:0000313|EMBL:AGK24641.1}; RN [1] {ECO:0000313|EMBL:AGK24641.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K56-2 {ECO:0000313|EMBL:AGK24641.1}; RX PubMed=24841205; DOI=10.1074/jbc.M114.562603; RA Hanuszkiewicz A., Pittock P., Humphries F., Moll H., Rosales A.R., RA Molinaro A., Moynagh P.N., Lajoie G.A., Valvano M.A.; RT "Identification of the Flagellin Glycosylation System in Burkholderia RT cenocepacia and the Contribution of Glycosylated Flagellin to Evasion of RT Human Innate Immune Responses."; RL J. Biol. Chem. 289:19231-19244(2014). CC -!- FUNCTION: Flagellin is the subunit protein which polymerizes to form CC the filaments of bacterial flagella. {ECO:0000256|RuleBase:RU362073}. CC -!- SUBCELLULAR LOCATION: Bacterial flagellum CC {ECO:0000256|ARBA:ARBA00004365, ECO:0000256|RuleBase:RU362073}. CC Secreted {ECO:0000256|ARBA:ARBA00004613, CC ECO:0000256|RuleBase:RU362073}. CC -!- SIMILARITY: Belongs to the bacterial flagellin family. CC {ECO:0000256|ARBA:ARBA00005709, ECO:0000256|RuleBase:RU362073}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KC763156; AGK24641.1; -; Genomic_DNA. DR RefSeq; WP_006491903.1; NZ_UARA01000004.1. DR EnsemblBacteria; OOA16569; OOA16569; A8F55_09600. DR GeneID; 56556672; -. DR PATRIC; fig|95486.65.peg.2941; -. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.8.410; -; 1. DR InterPro; IPR001492; Flagellin. DR InterPro; IPR042187; Flagellin_C_sub2. DR InterPro; IPR001029; Flagellin_D0/D1. DR InterPro; IPR022578; Flagellin_DUF. DR Pfam; PF00700; Flagellin_C; 1. DR Pfam; PF00669; Flagellin_N; 1. DR Pfam; PF12613; FliC_SP; 1. DR PRINTS; PR00207; FLAGELLIN. PE 3: Inferred from homology; KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143, KW ECO:0000256|RuleBase:RU362073}; KW Cell projection {ECO:0000313|EMBL:AGK24641.1}; KW Cilium {ECO:0000313|EMBL:AGK24641.1}; KW Flagellum {ECO:0000313|EMBL:AGK24641.1}; KW Secreted {ECO:0000256|RuleBase:RU362073}. SQ SEQUENCE 384 AA; 38757 MW; C381F1EB591FA35B CRC64; MLGINSNINS LVAQQNLNGS QNALSQAITR LSSGKRINSA ADDAAGLAIS TRMQTQINGL NQGVSNANDG VSMIQTASSA LSSLTNSLQR IRQLAVQAST GTMSTTDQAA LQQEVSQQIQ EVNRIASQTT YNGTNILDGS AGIVSFQVGA NVGQTISLDL SQSMSAAKIG GGLVQKGQTV GTVTGLSLDN NGAYTGSGAT ITAINVLSDG KGGYTFTDQN GGAISQTVAQ SVFGANATTG TGTAVGNLTL QSGATGAGTS AAQQTAITNA IAQINAVNKP ATVSNLDIST VSGANVAMVS IDNALQTVNN VQAALGAAQN RFTAIATSQQ AESTDLSSAQ SQITDANFAQ ETANMSKNQV LQQAGISVLA QANSLPQQVL KLLQ //