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Database: UniProt
Entry: A0A068QSL8_9GAMM
LinkDB: A0A068QSL8_9GAMM
Original site: A0A068QSL8_9GAMM 
ID   A0A068QSL8_9GAMM        Unreviewed;       356 AA.
AC   A0A068QSL8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Flagellin {ECO:0000256|RuleBase:RU362073};
GN   Name=fliC {ECO:0000313|EMBL:CDG17998.1};
GN   ORFNames=XDD1_2299 {ECO:0000313|EMBL:CDG17998.1};
OS   Xenorhabdus doucetiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG17998.1, ECO:0000313|Proteomes:UP000032721};
RN   [1] {ECO:0000313|EMBL:CDG17998.1, ECO:0000313|Proteomes:UP000032721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA   Genoscope - CEA;
RL   Submitted (JUL-2013) 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|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; FO704550; CDG17998.1; -; Genomic_DNA.
DR   RefSeq; WP_045971021.1; NZ_VNHN01000004.1.
DR   AlphaFoldDB; A0A068QSL8; -.
DR   STRING; 351671.XDD1_2299; -.
DR   KEGG; xdo:XDD1_2299; -.
DR   HOGENOM; CLU_011142_7_2_6; -.
DR   OrthoDB; 9796789at2; -.
DR   Proteomes; UP000032721; 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:CDG17998.1};
KW   Cilium {ECO:0000313|EMBL:CDG17998.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Flagellum {ECO:0000313|EMBL:CDG17998.1};
KW   Secreted {ECO:0000256|RuleBase:RU362073}.
FT   DOMAIN          5..140
FT                   /note="Flagellin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00669"
FT   DOMAIN          271..355
FT                   /note="Flagellin C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00700"
FT   COILED          75..102
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          291..318
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   356 AA;  38235 MW;  5EBDC2D56828DB62 CRC64;
     MASVINTNYS ALQAQNNLNR SQGVLTNAIA RLSSGLRINS AKDDAAGQAI ANRFTANVKG
     LSQASRNAND GISIAQTTEG SLNEINNNLQ RIRELSVQAQ NESNSASDKK SIQDEVKLRL
     EEINRISEQT QFNGVKVLSQ DRKMTIQVGA HDGETIEIDL KEINSKKLGL AKFSVTPSAP
     HADNKLEKPA TGAATKFDFT EAKIAGLNLK DMEVHHAVDK DGNEDKTKYV LQGVNAKGET
     EYHSVAVNGA DGKLSTPTKL DATEPTAKPL ETLDAALSKV DTLRSSLGAV QNRLESTVNN
     LNNTVNNLSA ARSRIEDADY ATEVSNMSRG QILQQAGTAV LAQANQIPQT AMSLLR
//
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