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Database: UniProt
Entry: A0A0G3BNG8_9BURK
LinkDB: A0A0G3BNG8_9BURK
Original site: A0A0G3BNG8_9BURK 
ID   A0A0G3BNG8_9BURK        Unreviewed;       400 AA.
AC   A0A0G3BNG8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Flagellin {ECO:0000256|RuleBase:RU362073};
GN   Name=fliC {ECO:0000313|EMBL:AKJ30994.1};
GN   ORFNames=AAW51_4303 {ECO:0000313|EMBL:AKJ30994.1};
OS   Caldimonas brevitalea.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Caldimonas.
OX   NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ30994.1, ECO:0000313|Proteomes:UP000035352};
RN   [1] {ECO:0000313|EMBL:AKJ30994.1, ECO:0000313|Proteomes:UP000035352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ30994.1,
RC   ECO:0000313|Proteomes:UP000035352};
RA   Tang B., Yu Y.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Flagellin is the subunit protein which polymerizes to form
CC       the filaments of bacterial flagella. {ECO:0000256|RuleBase:RU362073}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362073}.
CC       Bacterial flagellum {ECO:0000256|RuleBase:RU362073}.
CC   -!- SIMILARITY: Belongs to the bacterial flagellin family.
CC       {ECO:0000256|ARBA:ARBA00005709, ECO:0000256|RuleBase:RU362073}.
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DR   EMBL; CP011371; AKJ30994.1; -; Genomic_DNA.
DR   RefSeq; WP_047196228.1; NZ_CP011371.1.
DR   AlphaFoldDB; A0A0G3BNG8; -.
DR   STRING; 413882.AAW51_4303; -.
DR   KEGG; pbh:AAW51_4303; -.
DR   PATRIC; fig|413882.6.peg.4498; -.
DR   OrthoDB; 9796789at2; -.
DR   Proteomes; UP000035352; Chromosome.
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   Gene3D; 3.30.70.2120; -; 1.
DR   Gene3D; 1.20.1330.10; f41 fragment of flagellin, N-terminal domain; 1.
DR   Gene3D; 6.10.10.10; Flagellar export chaperone, C-terminal domain; 1.
DR   InterPro; IPR001492; Flagellin.
DR   InterPro; IPR046358; Flagellin_C.
DR   InterPro; IPR042187; Flagellin_C_sub2.
DR   InterPro; IPR001029; Flagellin_N.
DR   PANTHER; PTHR42792; FLAGELLIN; 1.
DR   PANTHER; PTHR42792:SF2; FLAGELLIN; 1.
DR   Pfam; PF00700; Flagellin_C; 1.
DR   Pfam; PF00669; Flagellin_N; 1.
DR   PRINTS; PR00207; FLAGELLIN.
DR   SUPFAM; SSF64518; Phase 1 flagellin; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143,
KW   ECO:0000256|RuleBase:RU362073};
KW   Cell projection {ECO:0000313|EMBL:AKJ30994.1};
KW   Cilium {ECO:0000313|EMBL:AKJ30994.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Flagellum {ECO:0000313|EMBL:AKJ30994.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035352};
KW   Secreted {ECO:0000256|RuleBase:RU362073}.
FT   DOMAIN          5..142
FT                   /note="Flagellin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00669"
FT   DOMAIN          313..398
FT                   /note="Flagellin C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00700"
FT   COILED          102..129
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   400 AA;  41607 MW;  B97949E0BA17720B CRC64;
     MPQTINTNIA SLTAQRNLNS SQSSLSTSMQ RLSSGLRVNS AKDDAAGLAI AERMSTQVRG
     LNVAARNAND GISLAQVAEG ALGKVSDMLQ RMRELAVQSA NATNSTDDRK ALQAEVSQLR
     DEINRVAKQT AFNGQKLLDG SFSAATFQVG ANSGESITIA ALTDASADGL SKVVYGEASE
     ADIDASAITD LGAITDGSLV VTVGTEAFTL GDLAVARTGA ERMGQVVEAI NRRTSDTGVA
     AFLQQEDDGQ YTVQLRSSNL DADGSAVAVT LAGFATATTG LTTTPAITNS DATSTAGIDE
     LSIETVEDAW LALKQIDDSL DQINEARATL GAVQSRFENA VSNIQIQSEN TAAARGRIMD
     ADFAAETANM SRAQILQQAG TAMVAQANQL PQQVLKLLQG
//
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