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Database: UniProt
Entry: A0A1X7GPC4_9SPHN
LinkDB: A0A1X7GPC4_9SPHN
Original site: A0A1X7GPC4_9SPHN 
ID   A0A1X7GPC4_9SPHN        Unreviewed;       269 AA.
AC   A0A1X7GPC4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Flagellin {ECO:0000256|RuleBase:RU362073};
GN   ORFNames=SAMN06295910_2042 {ECO:0000313|EMBL:SMF72592.1};
OS   Allosphingosinicella indica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Allosphingosinicella.
OX   NCBI_TaxID=941907 {ECO:0000313|EMBL:SMF72592.1, ECO:0000313|Proteomes:UP000192934};
RN   [1] {ECO:0000313|Proteomes:UP000192934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dd16 {ECO:0000313|Proteomes:UP000192934};
RA   Varghese N., Submissions S.;
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; LT840185; SMF72592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7GPC4; -.
DR   STRING; 941907.SAMN06295910_2042; -.
DR   OrthoDB; 9796789at2; -.
DR   Proteomes; UP000192934; Chromosome i.
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:SMF72592.1};
KW   Cilium {ECO:0000313|EMBL:SMF72592.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Flagellum {ECO:0000313|EMBL:SMF72592.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192934};
KW   Secreted {ECO:0000256|RuleBase:RU362073}.
FT   DOMAIN          4..137
FT                   /note="Flagellin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00669"
FT   DOMAIN          183..268
FT                   /note="Flagellin C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00700"
FT   COILED          74..128
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   269 AA;  27872 MW;  E4EB9614EB2D55F9 CRC64;
     MTVINTNTSA LRAQNGGRVA EQSLRVAMER LSTGKRINSS KDDAAGLAIA SSMTSQIRGM
     NQAIRNSNDG ISLAQTAEGA LNEVTNMLQR IRELAVQSAS GTYSDDDRTN LQEEVKALGA
     QINDIVANTK FNGVTLFGSA DGSFAIQTGA NSGDQVTISI TGLDVSSASG ADISSVSGAE
     SALDDVDTAL KDVGTVRAGL GAAQSRLEST VNNLTNNVTN LADARSRIED ADFSAETTNL
     AKAQILSQAS TAMLAQANQS QQGVLSLLR
//
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