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Database: UniProt
Entry: A0A1M5RLV1_9FIRM
LinkDB: A0A1M5RLV1_9FIRM
Original site: A0A1M5RLV1_9FIRM 
ID   A0A1M5RLV1_9FIRM        Unreviewed;       390 AA.
AC   A0A1M5RLV1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Flagellin {ECO:0000256|ARBA:ARBA00020110, ECO:0000256|RuleBase:RU362073};
GN   ORFNames=SAMN02745221_02063 {ECO:0000313|EMBL:SHH27304.1};
OS   Thermosyntropha lipolytica DSM 11003.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Thermosyntropha.
OX   NCBI_TaxID=1123382 {ECO:0000313|EMBL:SHH27304.1, ECO:0000313|Proteomes:UP000242329};
RN   [1] {ECO:0000313|Proteomes:UP000242329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11003 {ECO:0000313|Proteomes:UP000242329};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) 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; FQWY01000052; SHH27304.1; -; Genomic_DNA.
DR   RefSeq; WP_073093431.1; NZ_FQWY01000052.1.
DR   AlphaFoldDB; A0A1M5RLV1; -.
DR   STRING; 1123382.SAMN02745221_02063; -.
DR   OrthoDB; 9796789at2; -.
DR   Proteomes; UP000242329; 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; 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:SHH27304.1};
KW   Cilium {ECO:0000313|EMBL:SHH27304.1};
KW   Flagellum {ECO:0000313|EMBL:SHH27304.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242329};
KW   Secreted {ECO:0000256|RuleBase:RU362073}.
FT   DOMAIN          3..140
FT                   /note="Flagellin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00669"
FT   DOMAIN          305..389
FT                   /note="Flagellin C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00700"
SQ   SEQUENCE   390 AA;  41479 MW;  B126278240A9F893 CRC64;
     MIINHNLMAM NTHRQLSINN TMAQKSIEKL SSGFRINRAG DDAAGLAISE KMRGQIRGLT
     QASRNAQDAI SLIQTAEGAL NEVHAILQRM RELAVQAAND TNTTVDRGEI QKEINQLTSE
     IDRIANTTEF NTQKLLDGSK KGLVEAKDAE IIFQNNSSAN LQVSTAAINA ASIIATGGTI
     TITRVNASTG FEATDFRIGN PAGVAVTLVG ANEIQWAGVS LANFFAGGTL TALQVGESIT
     ISIKARVEGS TDISSALSMQ IGANTGQNIT VGINSMKAVD LGLRQTAGGA ALDITDYDKA
     TAAITTINNA LETVSTERSK LGAIQNRLEH TIKNLDTSAE NLQAAESRIR DVDMAKEMMN
     FTKQNILQQA ATAMLAQANQ APQTVLQLLR
//
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