ID   FM3_BORPE               Reviewed;         204 AA.
AC   P17835;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Serotype 3 fimbrial subunit;
DE   Flags: Precursor;
GN   Name=fim3; OrderedLocusNames=BP1568;
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=Johama / Serotype 3;
RX   PubMed=1969830; DOI=10.1016/0378-1097(90)90307-c;
RA   Mooi F.R., Ter Avest A., van der Heide H.G.J.;
RT   "Structure of the Bordetella pertussis gene coding for the serotype 3
RT   fimbrial subunit.";
RL   FEMS Microbiol. Lett. 54:327-331(1990).
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; X51543; CAA35920.1; -; Genomic_DNA.
DR   EMBL; BX640415; CAE41857.1; -; Genomic_DNA.
DR   PIR; S10882; S10882.
DR   PIR; S12578; S12578.
DR   RefSeq; NP_880302.1; NC_002929.2.
DR   RefSeq; WP_010930436.1; NZ_CP039022.1.
DR   AlphaFoldDB; P17835; -.
DR   SMR; P17835; -.
DR   STRING; 257313.BP1568; -.
DR   GeneID; 45390109; -.
DR   KEGG; bpe:BP1568; -.
DR   PATRIC; fig|257313.5.peg.1683; -.
DR   eggNOG; COG3539; Bacteria.
DR   HOGENOM; CLU_088965_2_0_4; -.
DR   OMA; IENTCTV; -.
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..25
FT   CHAIN           26..204
FT                   /note="Serotype 3 fimbrial subunit"
FT                   /id="PRO_0000009152"
FT   DISULFID        41..84
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   204 AA;  21803 MW;  93171E86BDE02D7A CRC64;
     MSKFSYPALR AALILAASPV LPALANDGTI VITGSISDQT CVIEEPSTLN HIKVVQLPKI
     SKNALRNDGD TAGATPFDIK LKECPQALGA LKLYFEPGIT TNYDTGDLIA YKQTYNASGN
     GNLSTVSSAT KAKGVEFRLA NLNGQHIRMG TDKTTQAAQT FTGKVTNGSK SYTLRYLASY
     VKKPKEDVDA AQITSYVGFS VVYP