FLID_AQUAE
ID FLID_AQUAE Reviewed; 441 AA.
AC O67805;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Flagellar hook-associated protein 2;
DE Short=HAP2;
DE AltName: Full=Filament cap protein;
DE AltName: Full=Flagellar cap protein;
GN Name=fliD; OrderedLocusNames=aq_2001;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Required for the 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Bacterial flagellum.
CC -!- SIMILARITY: Belongs to the FliD family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07765.1; -; Genomic_DNA.
DR PIR; A70472; A70472.
DR RefSeq; NP_214374.1; NC_000918.1.
DR RefSeq; WP_010881310.1; NC_000918.1.
DR AlphaFoldDB; O67805; -.
DR SMR; O67805; -.
DR STRING; 224324.aq_2001; -.
DR EnsemblBacteria; AAC07765; AAC07765; aq_2001.
DR KEGG; aae:aq_2001; -.
DR eggNOG; COG1345; Bacteria.
DR HOGENOM; CLU_051679_0_0_0; -.
DR InParanoid; O67805; -.
DR OMA; DWGMTER; -.
DR OrthoDB; 883503at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0009421; C:bacterial-type flagellum filament cap; IBA:GO_Central.
DR GO; GO:0009424; C:bacterial-type flagellum hook; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IBA:GO_Central.
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; PTHR30288; 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; Coiled coil; Reference proteome; Secreted.
FT CHAIN 1..441
FT /note="Flagellar hook-associated protein 2"
FT /id="PRO_0000177012"
FT COILED 376..416
FT /evidence="ECO:0000255"
SQ SEQUENCE 441 AA; 49461 MW; 55985689485907F4 CRC64;
MAGELYFSGV TGAYDWGSVL DNIMAVKSIP IQKLQQKKQL INQKLQILGE FSQKLSDLKN
LIENFNLESA LKTKKADVSD SDVISVSVSE NAPEISFSVN VLNTASKEIL VYDAGFNSLD
ETIGSDGSFT LRYYTSPTDY VEYTIDYSLI DTLKDIVNKI NETQDYVKAS IYYDGNKYKL
MLAETSEENS TVETAPDLST KAIHLLGTLP HQFGNNVLIQ QAKNARIQIG SGDVIESAGN
TFENVIEGVS ISAKRAGTSE VSISQDFSKI REFLNNFVKS YNEVVSQVKS LTLGENAPFR
GENTIMNVKY GLSDTLTPLM ELGLIEYKED GTISLSGNLE SVINEKPDEF KLKMTQFLES
AKAVAKVNYE AFEDFKEYLN DQAERIDENI RLLSQRLVQE EQILKRQFAQ LEDFMNYANQ
IRERLKQFMV SISEMNGGNN K