ID   FM2_BORPE               Reviewed;         207 AA.
AC   P05788;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Serotype 2 fimbrial subunit;
DE   Flags: Precursor;
GN   Name=fim2; OrderedLocusNames=BP1119;
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=Wellcome 28;
RX   PubMed=2897065; DOI=10.1111/j.1365-2958.1987.tb00513.x;
RA   Livey I., Duggleby C.J., Robinson A.;
RT   "Cloning and nucleotide sequence analysis of the serotype 2 fimbrial
RT   subunit gene of Bordetella pertussis.";
RL   Mol. Microbiol. 1:203-209(1987).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE41417.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Y00527; CAA68585.1; -; Genomic_DNA.
DR   EMBL; BX640414; CAE41417.1; ALT_INIT; Genomic_DNA.
DR   PIR; S03754; S03754.
DR   RefSeq; NP_879898.1; NC_002929.2.
DR   RefSeq; WP_010930199.1; NZ_CP039022.1.
DR   RefSeq; WP_019248935.1; NZ_CP039021.1.
DR   AlphaFoldDB; P05788; -.
DR   SMR; P05788; -.
DR   STRING; 257313.BP1119; -.
DR   GeneID; 45388899; -.
DR   KEGG; bpe:BP1119; -.
DR   PATRIC; fig|257313.5.peg.1198; -.
DR   eggNOG; COG3539; Bacteria.
DR   HOGENOM; CLU_088965_2_0_4; -.
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..26
FT   CHAIN           27..207
FT                   /note="Serotype 2 fimbrial subunit"
FT                   /id="PRO_0000009151"
FT   DISULFID        42..85
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   207 AA;  21950 MW;  0CFFF8384E6B2405 CRC64;
     MQIPFQRALR LCLRAALAAI ASAAHADDGT IVITGTITDT TCVIEDPSGP NHTKVVQLPK
     ISKNALKANG DQAGRTPFII KLKDCPSSLG NGVKAYFEPG PTTDYSTGDL RAYKMVYATN
     PQTQLSNITA ATEAQGVQVR ISNLNDSKIT MGANEATQQA AGFDPEVQTG GTSRTVTMRY
     LASYVKKNGD VEASAITTYV GFSVVYP