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Database: UniProt
Entry: A0A1W1UNH5_DESTI
LinkDB: A0A1W1UNH5_DESTI
Original site: A0A1W1UNH5_DESTI 
ID   A0A1W1UNH5_DESTI        Unreviewed;       553 AA.
AC   A0A1W1UNH5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Flagellin {ECO:0000256|ARBA:ARBA00020110, ECO:0000256|RuleBase:RU362073};
GN   ORFNames=SAMN00017405_0950 {ECO:0000313|EMBL:SMB82652.1};
OS   Desulfonispora thiosulfatigenes DSM 11270.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfonispora.
OX   NCBI_TaxID=656914 {ECO:0000313|EMBL:SMB82652.1, ECO:0000313|Proteomes:UP000192731};
RN   [1] {ECO:0000313|EMBL:SMB82652.1, ECO:0000313|Proteomes:UP000192731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11270 {ECO:0000313|EMBL:SMB82652.1,
RC   ECO:0000313|Proteomes:UP000192731};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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; FWWT01000008; SMB82652.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1UNH5; -.
DR   STRING; 656914.SAMN00017405_0950; -.
DR   Proteomes; UP000192731; Unassembled WGS sequence.
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; 2.
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:SMB82652.1};
KW   Cilium {ECO:0000313|EMBL:SMB82652.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Flagellum {ECO:0000313|EMBL:SMB82652.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192731};
KW   Secreted {ECO:0000256|RuleBase:RU362073}.
FT   DOMAIN          9..133
FT                   /note="Flagellin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00669"
FT   DOMAIN          467..552
FT                   /note="Flagellin C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00700"
FT   COILED          94..121
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   553 AA;  57763 MW;  A80C43ED8B56B23C CRC64;
     MIFEVAFRQM NGATTAQSKS MEKLSSGLRI NKAGDDAAGL AISEKMRGQI RGLNQASANA
     QDGISMVQTA EGALNETHSI LQRVRELADQ SANGTNTAED RKAIQDEVKQ LKEEIDRIGN
     TTEFNTQKLL NGNLQSSGAT IGTNSTTSAV VGKLEAGKMT AAQALAADLS STTFQKDTFN
     IDGHSIEVNW DTLLTTEQKD KIKAIGAGSN ISQLSSVKDL ITSKINEAID QYNAQNPAGA
     TVQHVEGYLD SATAATAKLV IKSGTEGTDS VVALTTKGAA TSVGALIMSD TAGDVTADAS
     TNTGTNKFNG STVSSGATFE MDLNGVKMKV ATGSDIENNT TTMDAAATAL QTAIKTAVDS
     YNTLQGKSAG EEGYVEQVKV NATKDGRFEI TSESGTVTFK DYEGKTSVKD LGLTQAQTDA
     SGNGGMTFQI GANKGQTITF GINDMRTSAL GISGVDASTQ SGASLALESI DKAIKNVSAE
     RSKLGAIQNR LEHTINNLGT SSENLTAAES RVRDVDMAKE IMESTKNGIL AQAAQAMMAQ
     ANSMPQGILQ LLR
//
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