ID E1X2Q7_HALMS Unreviewed; 282 AA.
AC E1X2Q7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Flagellin {ECO:0000256|RuleBase:RU362073};
GN Name=fliC3 {ECO:0000313|EMBL:CBW25102.1};
GN Synonyms=flaA {ECO:0000313|EMBL:CBW25102.1}, hag
GN {ECO:0000313|EMBL:CBW25102.1};
GN OrderedLocusNames=BMS_0168 {ECO:0000313|EMBL:CBW25102.1};
OS Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS (Bacteriovorax marinus).
OC Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC Halobacteriovoraceae; Halobacteriovorax.
OX NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW25102.1, ECO:0000313|Proteomes:UP000008963};
RN [1] {ECO:0000313|Proteomes:UP000008963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC {ECO:0000313|Proteomes:UP000008963};
RX PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA Williams H.N., Stine O.C.;
RT "A small predatory core genome in the divergent marine Bacteriovorax
RT marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL ISME J. 7:148-160(2013).
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; FQ312005; CBW25102.1; -; Genomic_DNA.
DR RefSeq; WP_014242891.1; NC_016620.1.
DR AlphaFoldDB; E1X2Q7; -.
DR STRING; 862908.BMS_0168; -.
DR KEGG; bmx:BMS_0168; -.
DR PATRIC; fig|862908.3.peg.162; -.
DR eggNOG; COG1344; Bacteria.
DR HOGENOM; CLU_011142_2_2_7; -.
DR Proteomes; UP000008963; 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:CBW25102.1};
KW Cilium {ECO:0000313|EMBL:CBW25102.1};
KW Flagellum {ECO:0000313|EMBL:CBW25102.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008963};
KW Secreted {ECO:0000256|RuleBase:RU362073}.
FT DOMAIN 5..141
FT /note="Flagellin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00669"
FT DOMAIN 192..276
FT /note="Flagellin C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00700"
SQ SEQUENCE 282 AA; 29672 MW; 65075542F36FFD97 CRC64;
MGLRINTNVA SLNAQRNLSG TRINMNKSLE KLSSGQRINR AGDDAAGLAI SENLKAQIKG
LGQAKRNAED GISLVQIAEG ALGEVSNILI RLRELSVQAA SDTIGATERK FLNVEFEQLT
SEMDRIANST EFNRVPLLNG TGAVFDIQIG TRNDPISDRL TFDASSADVN VAALGLNLAS
VADKISSQNS LSSIDSAIVS VSGIRADFGA LQNRLQSTIN NIAVSVENLS AANSRVRDTD
IAAETAELTK QNILMTAGTS VLSQANSSTK NALSLIQSAS QG
//