ID   FMFX_BORPE              Reviewed;         201 AA.
AC   P09808;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2003, sequence version 2.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Fimbrial protein FimX;
DE   AltName: Full=Pilin;
DE   Flags: Precursor;
GN   Name=fimX; OrderedLocusNames=BP2674;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SA1;
RX   PubMed=2902506; DOI=10.1111/j.1365-2958.1988.tb00061.x;
RA   Pedroni P., Riboli B., de Ferra F., Grandi G., Toma S., Arico B.,
RA   Rappuoli R.;
RT   "Cloning of a novel pilin-like gene from Bordetella pertussis: homology to
RT   the fim2 gene.";
RL   Mol. Microbiol. 2:539-543(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Bordetella pertussis is the causative agent of whooping
CC       cough. An essential step in the disease process is the attachment of
CC       the bacteria to the ciliated epithelium of the respiratory tract,
CC       enabling the organism to resist normal host-clearance mechanisms. It is
CC       unclear which bacterial cell surface component are responsible for
CC       adherence but the fimbriae of B.pertussis are prime candidates for
CC       being involved in this process.
CC   -!- SUBCELLULAR LOCATION: Fimbrium. Note=Pili structure on the cell
CC       surface.
CC   -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR   EMBL; Y00556; CAA68634.1; -; Genomic_DNA.
DR   EMBL; BX640419; CAE42950.1; -; Genomic_DNA.
DR   PIR; S01929; S01929.
DR   RefSeq; NP_881287.1; NC_002929.2.
DR   RefSeq; WP_010931071.1; NZ_CP039022.1.
DR   AlphaFoldDB; P09808; -.
DR   SMR; P09808; -.
DR   STRING; 257313.BP2674; -.
DR   GeneID; 45389666; -.
DR   KEGG; bpe:BP2674; -.
DR   PATRIC; fig|257313.5.peg.2880; -.
DR   eggNOG; COG3539; Bacteria.
DR   HOGENOM; CLU_088965_2_0_4; -.
DR   OMA; GGQYYAL; -.
DR   Proteomes; UP000002676; Chromosome.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   Gene3D; 2.60.40.1090; -; 1.
DR   InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR   InterPro; IPR008966; Adhesion_dom_sf.
DR   InterPro; IPR039458; FimA-like.
DR   Pfam; PF16970; FimA; 1.
DR   SUPFAM; SSF49401; SSF49401; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Fimbrium; Reference proteome; Signal.
FT   SIGNAL          1..21
FT   CHAIN           22..201
FT                   /note="Fimbrial protein FimX"
FT                   /id="PRO_0000009153"
FT   DISULFID        37..79
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165..166
FT                   /note="AK -> GQ (in Ref. 1; CAA68634)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   201 AA;  21462 MW;  F47670CC055B03F6 CRC64;
     MQAKTFLLGA ALAGVALAAH AEDGTIVITG TITDQTCTIE DPSPGYIKVV HLPTISKSAL
     KNAGDVAGRT RFDIKLKDCP TTVNTLKLYF EPGPTTDYGT KDLKAYKQAW YVDAATLLKS
     PPSVTEAKGV QIRLMNLNGK QIPMGETEPN QHAAAFSGTM QAGQAKKSFT LHYLAGYVKK
     ASGEVEATML TTYVGFSVVY P