ID A0A1H0EWC9_9GAMM Unreviewed; 465 AA.
AC A0A1H0EWC9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN04487957_102217 {ECO:0000313|EMBL:SDN86579.1};
OS Halomonas shengliensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=419597 {ECO:0000313|EMBL:SDN86579.1, ECO:0000313|Proteomes:UP000199075};
RN [1] {ECO:0000313|Proteomes:UP000199075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6444 {ECO:0000313|Proteomes:UP000199075};
RA Varghese N., Submissions S.;
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; FNIV01000002; SDN86579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0EWC9; -.
DR STRING; 419597.SAMN04487957_102217; -.
DR OrthoDB; 5980200at2; -.
DR Proteomes; UP000199075; 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:SDN86579.1};
KW Cilium {ECO:0000313|EMBL:SDN86579.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362066};
KW Flagellum {ECO:0000313|EMBL:SDN86579.1};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 11..105
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 221..445
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
FT COILED 401..428
FT /evidence="ECO:0000256|RuleBase:RU362066"
SQ SEQUENCE 465 AA; 48924 MW; EA7B48B2F140251A CRC64;
MATISSLGIG SGLDLNGLLD QLRDAERGKL EPIKAQQAQQ EARISAFGRL QSALTTFQES
VDKLNDASLY QSLSANVRGE AFTAKAGSEA QPGSFSVEVG KLATAGTLAT QRVASADQPI
VDQAALDASA GKLVLNFVGG DVPVVKVDIT ANSTLEDIRD AINARDDAGV SASIVHDGSG
YRLALNSKET GAEASIDSTN FEDLVVGNLA TEPGAIVTQT GQDAALKVNG IDITSASNTV
EGAIQGVTLT LNATTAEGQP DTLRVEQDTL KVREAVSGFV KAFNELKDTI GTLTSYDSES
GQAGELNGDR TVRTIESRLR AALSGGVGEG ELRMLGEVGI SLQRDGTLEL DDEALDELVS
GNMAALGEFF AGADEAGGLA GQVNGTLSQL LDDSGLVNRS IEGAEGRLER LDERYGRMEQ
SIERTIERYR VQFGQLDAMI AQMNQTSEYL TQQFDALDAQ LGRKK
//
