FLID2_PSEAE
ID FLID2_PSEAE Reviewed; 474 AA.
AC Q9K3C5; P72153;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=B-type flagellar hook-associated protein 2;
DE Short=HAP2;
DE AltName: Full=Filament cap protein;
DE AltName: Full=Flagellar cap protein;
GN Name=fliD; OrderedLocusNames=PA1094;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1244,
RC ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101
RC / PAO1, and CS29;
RX PubMed=10678962; DOI=10.1128/iai.68.3.1474-1479.2000;
RA Arora S.K., Dasgupta N., Lory S., Ramphal R.;
RT "Identification of two distinct types of flagellar cap proteins, FliD, in
RT Pseudomonas aeruginosa.";
RL Infect. Immun. 68:1474-1479(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-148.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Wahl S.A., Baker N.R.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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. Essential for motility. Responsible for adhesion to
CC mucin, which is the initial event in colonization by this organism of
CC the airways of cystic fibrosis patients.
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; AF139821; AAF35976.1; -; Genomic_DNA.
DR EMBL; AF139819; AAF35974.1; -; Genomic_DNA.
DR EMBL; AF139820; AAF35975.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04483.1; -; Genomic_DNA.
DR EMBL; U54775; AAA99809.1; -; Genomic_DNA.
DR PIR; G83507; G83507.
DR RefSeq; NP_249785.1; NC_002516.2.
DR RefSeq; WP_003082190.1; NZ_QZGE01000006.1.
DR PDB; 5FHY; X-ray; 2.20 A; A/B=78-405.
DR PDBsum; 5FHY; -.
DR AlphaFoldDB; Q9K3C5; -.
DR SMR; Q9K3C5; -.
DR STRING; 208964.PA1094; -.
DR PaxDb; Q9K3C5; -.
DR PRIDE; Q9K3C5; -.
DR EnsemblBacteria; AAG04483; AAG04483; PA1094.
DR GeneID; 881775; -.
DR KEGG; pae:PA1094; -.
DR PATRIC; fig|208964.12.peg.1133; -.
DR PseudoCAP; PA1094; -.
DR HOGENOM; CLU_015182_5_0_6; -.
DR InParanoid; Q9K3C5; -.
DR OMA; TLEWQRD; -.
DR PhylomeDB; Q9K3C5; -.
DR BioCyc; PAER208964:G1FZ6-1117-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009421; C:bacterial-type flagellum filament cap; IDA:PseudoCAP.
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; IDA:PseudoCAP.
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 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum; Coiled coil; Reference proteome;
KW Secreted.
FT CHAIN 1..474
FT /note="B-type flagellar hook-associated protein 2"
FT /id="PRO_0000177022"
FT COILED 408..454
FT /evidence="ECO:0000255"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:5FHY"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:5FHY"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:5FHY"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 173..184
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:5FHY"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:5FHY"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 239..252
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:5FHY"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:5FHY"
FT TURN 297..300
FT /evidence="ECO:0007829|PDB:5FHY"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:5FHY"
SQ SEQUENCE 474 AA; 49450 MW; 0BDAC913DC9962D6 CRC64;
MAGISIGVGS TDYTDLVNKM VNLEGAAKTN QLATLEKTTT TRLTALGQFK SAISAFQTAL
TALNSNAVFM ARTAKSSNED ILKASATQSA VAGTYQIQVN SLATSSKIAL QAIADPANAK
FNSGTLNISV GDTKLPAITV DSSNNTLAGM RDAINQAGKE AGVSATIITD NSGSRLVLSS
TKTGDGKDIK VEVSDDGSGG NTSLSQLAFD PATAPKLSDG AAAGYVTKAA NGEITVDGLK
RSIASNSVSD VIDGVSFDVK AVTEAGKPIT LTVSRDDAGV KDNVKKFVEA YNTLTKFINE
QTVVTKVGED KNPVTGALLG DASVRALVNT MRSELIASNE NGSVRNLAAL GITTTKDGTL
EIDEKKLDKA ISADFEGVAS YFTGDTGLAK RLGDKMKPYT DAQGILDQRT TTLQKTLSNV
DTQKADLAKR LAALQEKLTT QFNLLSAMQD EMTKRQKSIT DNLASLPYGS GKKT
