ID A0A1G9X3E2_9BACI Unreviewed; 492 AA.
AC A0A1G9X3E2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Flagellar hook-associated protein 2 {ECO:0000256|RuleBase:RU362066};
DE Short=HAP2 {ECO:0000256|RuleBase:RU362066};
DE AltName: Full=Flagellar cap protein {ECO:0000256|RuleBase:RU362066};
GN ORFNames=SAMN05443253_106242 {ECO:0000313|EMBL:SDM90895.1};
OS Bacillus sp. OK048.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1882761 {ECO:0000313|EMBL:SDM90895.1, ECO:0000313|Proteomes:UP000199133};
RN [1] {ECO:0000313|EMBL:SDM90895.1, ECO:0000313|Proteomes:UP000199133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK048 {ECO:0000313|EMBL:SDM90895.1,
RC ECO:0000313|Proteomes:UP000199133};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for morphogenesis and for the elongation of the
CC flagellar filament by facilitating polymerization of the flagellin
CC monomers at the tip of growing filament. Forms a capping structure,
CC which prevents flagellin subunits (transported through the central
CC channel of the flagellum) from leaking out without polymerization at
CC the distal end. {ECO:0000256|RuleBase:RU362066}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000256|ARBA:ARBA00011255,
CC ECO:0000256|RuleBase:RU362066}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362066}.
CC Bacterial flagellum {ECO:0000256|RuleBase:RU362066}.
CC -!- SIMILARITY: Belongs to the FliD family. {ECO:0000256|ARBA:ARBA00009764,
CC ECO:0000256|RuleBase:RU362066}.
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DR EMBL; FNHN01000006; SDM90895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9X3E2; -.
DR STRING; 1882761.SAMN05443253_106242; -.
DR Proteomes; UP000199133; Unassembled WGS sequence.
DR GO; GO:0009421; C:bacterial-type flagellum filament cap; IEA:InterPro.
DR GO; GO:0009424; C:bacterial-type flagellum hook; IEA:UniProtKB-UniRule.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR InterPro; IPR010810; Flagellin_hook_IN_motif.
DR InterPro; IPR040026; FliD.
DR InterPro; IPR010809; FliD_C.
DR InterPro; IPR003481; FliD_N.
DR PANTHER; PTHR30288; FLAGELLAR CAP/ASSEMBLY PROTEIN FLID; 1.
DR PANTHER; PTHR30288:SF0; FLAGELLAR HOOK-ASSOCIATED PROTEIN 2; 1.
DR Pfam; PF07196; Flagellin_IN; 1.
DR Pfam; PF07195; FliD_C; 1.
DR Pfam; PF02465; FliD_N; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143,
KW ECO:0000256|RuleBase:RU362066};
KW Cell projection {ECO:0000313|EMBL:SDM90895.1};
KW Cilium {ECO:0000313|EMBL:SDM90895.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Flagellum {ECO:0000313|EMBL:SDM90895.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199133};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 1..95
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 219..479
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 492 AA; 53676 MW; F1BAD416D45CEAD6 CRC64;
MDTDSIVKKL MNAESISLNK LKQNQQKQTW LSDTYRQWNA DLLAFRSNTV LNMSLSKTYN
TFDVASSQEN SVSATAPGTS IAGTYSVEVK QLASSATFAG DKVSLDPTKS LGNSVQGAGQ
LTADTSIVMK VNNETVTLDI KTTDKINDVV AKINGAKDST GKSLGLQAFY DPTLQQFILK
TKETGVSSEI DLSMNTSPES QAFLKNTLGL DTTNLVATGQ NANVIFNGNE ITTLTSNHAT
IMGISFSFKS PTIGATTVTV SQNTDGVVKN IKDFVDQYNG LLEKINKAVS DPVYRDFQPL
LEEQKSEMSE KQIENWEEKA KSGLVRSDSI LSGLVTKMRS AMTSIVDNGS SYNSLSSIGI
SSRSYQDKGK LYVDETKLKE AIQADPDAVE KLFSQLGDSS KGTSGIINRI SETLQDGIKE
LTNKAGYTGN NQYDQSIIGK LLSNTQIDIT RQTVKLQRKE EQYYRQFAAM EQAMSRLNSQ
SSWLSQQMGG GM
//