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Database: UniProt
Entry: B8FJR9_DESAL
LinkDB: B8FJR9_DESAL
Original site: B8FJR9_DESAL 
ID   B8FJR9_DESAL            Unreviewed;       376 AA.
AC   B8FJR9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Flagellin {ECO:0000256|RuleBase:RU362073};
GN   OrderedLocusNames=Dalk_0642 {ECO:0000313|EMBL:ACL02347.1};
OS   Desulfatibacillum aliphaticivorans.
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfatibacillaceae; Desulfatibacillum.
OX   NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL02347.1, ECO:0000313|Proteomes:UP000000739};
RN   [1] {ECO:0000313|EMBL:ACL02347.1, ECO:0000313|Proteomes:UP000000739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK-01 {ECO:0000313|EMBL:ACL02347.1,
RC   ECO:0000313|Proteomes:UP000000739};
RX   PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA   Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA   Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT   "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT   for anaerobic alkane oxidation.";
RL   Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL02347.1; -; Genomic_DNA.
DR   RefSeq; WP_012609786.1; NC_011768.1.
DR   AlphaFoldDB; B8FJR9; -.
DR   KEGG; dal:Dalk_0642; -.
DR   eggNOG; COG1344; Bacteria.
DR   HOGENOM; CLU_011142_2_2_7; -.
DR   Proteomes; UP000000739; 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:ACL02347.1};
KW   Cilium {ECO:0000313|EMBL:ACL02347.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Flagellum {ECO:0000313|EMBL:ACL02347.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000739};
KW   Secreted {ECO:0000256|RuleBase:RU362073}.
FT   DOMAIN          6..142
FT                   /note="Flagellin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00669"
FT   DOMAIN          290..375
FT                   /note="Flagellin C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00700"
FT   COILED          101..128
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   376 AA;  39413 MW;  AF0223B3D4F4C0B4 CRC64;
     MGLRVANNIA AVNAHRQLGV TDSKVSKSLE RLSSGFRINR AKDDAAGLSM ARKFDAQVRS
     QAVAANNTTQ ANSLLQIAEG GVEQIDAILV RLKELSTQAA SKNNEQNLSD LNAEAQQLLT
     EMDRIANTTT FQGASLLTGY GTKGLVAADA GSVGSVSNMY DFDISNFKGT DAESIHFTSD
     GASVITMVYT GSGTVETQTL TVGSGGDTYD FSTFGVSFKT TTAADSAALA TSVASVGDTI
     TASVADATFQ VGETNSSDYR ISFQLNAMNQ TGLSVGNVDM STLANARSSL DMIDNAMTAL
     NASRAEIGAI QNRLDYTFAN LNIAIENNTA AMSVIQDVDM AMEMTTFTKN QILMQSGTAM
     LAQANSAPQN ILSLIG
//
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