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Database: UniProt
Entry: A0A097QWV6_HAFAL
LinkDB: A0A097QWV6_HAFAL
Original site: A0A097QWV6_HAFAL 
ID   A0A097QWV6_HAFAL        Unreviewed;       296 AA.
AC   A0A097QWV6;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Flagellin {ECO:0000256|RuleBase:RU362073};
GN   ORFNames=AT03_00090 {ECO:0000313|EMBL:AIU70957.1};
OS   Hafnia alvei FB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Hafnia.
OX   NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU70957.1, ECO:0000313|Proteomes:UP000029986};
RN   [1] {ECO:0000313|EMBL:AIU70957.1, ECO:0000313|Proteomes:UP000029986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB1 {ECO:0000313|EMBL:AIU70957.1,
RC   ECO:0000313|Proteomes:UP000029986};
RX   PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA   Tan J.Y., Yin W.F., Chan K.G.;
RT   "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT   pathogenesis: a draft genome perspective.";
RL   Gut Pathog. 6:29-29(2014).
CC   -!- FUNCTION: Flagellin is the subunit protein which polymerizes to form
CC       the filaments of bacterial flagella. {ECO:0000256|ARBA:ARBA00002270,
CC       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; CP009706; AIU70957.1; -; Genomic_DNA.
DR   RefSeq; WP_025799636.1; NZ_CP009706.1.
DR   AlphaFoldDB; A0A097QWV6; -.
DR   KEGG; hav:AT03_00090; -.
DR   PATRIC; fig|1453496.5.peg.23; -.
DR   eggNOG; COG1344; Bacteria.
DR   HOGENOM; CLU_011142_2_2_6; -.
DR   OrthoDB; 9796789at2; -.
DR   Proteomes; UP000029986; 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; 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:AIU70957.1};
KW   Cilium {ECO:0000313|EMBL:AIU70957.1};
KW   Flagellum {ECO:0000313|EMBL:AIU70957.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029986};
KW   Secreted {ECO:0000256|RuleBase:RU362073}.
FT   DOMAIN          5..141
FT                   /note="Flagellin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00669"
FT   DOMAIN          212..295
FT                   /note="Flagellin C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00700"
SQ   SEQUENCE   296 AA;  30480 MW;  738F483A510BA1B7 CRC64;
     MALSIFTNAS SMASTNALNK SNSLLSTSME RLGTGKRINS AADDAAGMQI ASRLQGQTNG
     MTVAKRNIAD ATSMLQTAEG AFDEVSNIMY RMKDLATQAA NDTNSTEDRA SLQSEFDQLN
     SELGNIMDNT SFGGTKLLSG GTGLASTGGL NFQIGSSNAE TLNVNVSSQL SGLTKTIGTA
     ATTNPSGTTV PDTGLGALEL DSAANASGAI ASLESALKDV GSLRSTLGAN INRLGHTSAN
     LANMQDNTEL ALGNIRDADF ASEASTMTRQ QMLAQTSMSM LKQSNSMSGM VMSLLG
//
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