FLID1_PSEAI
ID FLID1_PSEAI Reviewed; 478 AA.
AC O33421; Q51456; Q9LAG5; Q9LAG6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=A-type flagellar hook-associated protein 2;
DE Short=HAP2;
DE AltName: Full=Filament cap protein;
DE AltName: Full=Flagellar cap protein;
GN Name=fliD;
OS Pseudomonas aeruginosa.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=PAK;
RX PubMed=9488388; DOI=10.1128/iai.66.3.1000-1007.1998;
RA Arora S.K., Ritchings B.W., Almira E.C., Lory S., Ramphal R.;
RT "The Pseudomonas aeruginosa flagellar cap protein, FliD, is responsible for
RT mucin adhesion.";
RL Infect. Immun. 66:1000-1007(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29260 / PA103, CS2, CS32, and PAK;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 347-478.
RC STRAIN=DG1;
RA Wahl S.A., Darzins A., Baker N.R.;
RL Submitted (JUN-1995) 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. {ECO:0000269|PubMed:9488388}.
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; L81176; AAC09391.1; -; Genomic_DNA.
DR EMBL; AF139824; AAF35981.1; -; Genomic_DNA.
DR EMBL; AF139823; AAF35979.1; -; Genomic_DNA.
DR EMBL; AF139825; AAF35983.1; -; Genomic_DNA.
DR EMBL; AF139822; AAF35977.1; -; Genomic_DNA.
DR EMBL; L43064; AAA99299.1; -; Genomic_DNA.
DR RefSeq; WP_003123161.1; NZ_WXZX01000001.1.
DR RefSeq; WP_043083576.1; NZ_WCHW01000009.1.
DR AlphaFoldDB; O33421; -.
DR SMR; O33421; -.
DR PATRIC; fig|287.1479.peg.3135; -.
DR eggNOG; COG1345; Bacteria.
DR GO; GO:0009421; C:bacterial-type flagellum filament cap; IEA:InterPro.
DR GO; GO:0009424; C:bacterial-type flagellum hook; IEA:InterPro.
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; 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; Secreted.
FT CHAIN 1..478
FT /note="A-type flagellar hook-associated protein 2"
FT /id="PRO_0000177021"
FT COILED 409..460
FT /evidence="ECO:0000255"
FT VARIANT 166
FT /note="T -> S (in strain: PA103 and CS32)"
FT VARIANT 235
FT /note="K -> R (in strain: PA103)"
FT VARIANT 347..352
FT /note="TDVRML -> DLQACV (in strain: DG1)"
FT VARIANT 430
FT /note="E -> Q (in strain: PA103 and CS32)"
FT VARIANT 433
FT /note="N -> D (in strain: PA103)"
SQ SEQUENCE 478 AA; 50705 MW; A54C1FBCF9AE6579 CRC64;
MANSTTINGY NSGLDIKNIV STLVAAEKAP KEAQLKRLES DTTAKFTGIG QLKSAISDLQ
TILKELNKPE LFQKRSASTS DEKFATATAT KDALPGIYKL EVTQLASVSK VATASFADGY
KTTSGGTLTI KQGADDAGVT VNVAAGATLA EVRDSLNAQL KDKGITANIV NNPGDGTSRL
VFTGKDSGAG KDVFVQGSSG LENFNIGSVG ADGKLTLSQL DGTSSSSSGY ITQAKNAKFS
IDGLTLESPT NTVDKVINGV TFELKTVTDT NKPITISVEQ DRGGVKDNIK KFVEAYNKLV
GVTSELTGVT KVGDDKAPVV GALVGDSSVR NLLTTMRNEM VQPGQGTDVR MLADMGITTK
KDGTLEIDDK KLDKVLKDKF ESVSALFTGD TGLMKRLDDK LTPYTQTGGV LQQRLDGLQD
TIKSVDTQRE ALNRRVEQLQ DRLLKQFTAM DQLIGQLNQT SGRMAQALSS LPGLVKKS