ID   BFPA_ECO11              Reviewed;         193 AA.
AC   P58997;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Major structural subunit of bundle-forming pilus;
DE   AltName: Full=Bundle-forming pilin;
DE            Short=Bundlin;
DE   Flags: Precursor;
GN   Name=bfpA;
OS   Escherichia coli O111:H-.
OG   Plasmid pB171.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=168927;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O111:H- / B171 / EPEC;
RX   PubMed=8096320; DOI=10.1111/j.1365-2958.1993.tb01147.x;
RA   Sohel I., Puente J.L., Murray W.J., Vuopio-Varkila J., Schoolnik G.K.;
RT   "Cloning and characterization of the bundle-forming pilin gene of
RT   enteropathogenic Escherichia coli and its distribution in Salmonella
RT   serotypes.";
RL   Mol. Microbiol. 7:563-575(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 14-41, AND METHYLATION AT LEU-14.
RC   STRAIN=O111:H- / B171 / EPEC;
RX   PubMed=1683004; DOI=10.1126/science.1683004;
RA   Giron J.A., Ho A.S.Y., Schoolnik G.K.;
RT   "An inducible bundle-forming pilus of enteropathogenic Escherichia coli.";
RL   Science 254:710-713(1991).
CC   -!- FUNCTION: Major repeating bundle-forming pilus (BFP) subunit. Is
CC       required for EPEC localized adherence.
CC   -!- SUBUNIT: 10 to 100 laterally aligned filaments or bundle-forming pili
CC       coalesce into rope-like bundles. These form linkages between the
CC       bacteria within the enteropathogenic E.coli (EPEC) microcolonies that
CC       are attached to epithelial cells.
CC   -!- SUBCELLULAR LOCATION: Fimbrium. Membrane {ECO:0000255}; Single-pass
CC       membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=Ref.2; Type=Miscellaneous discrepancy; Note=The modified residue is misidentified as methionine.; Evidence={ECO:0000305|PubMed:1683004};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U27184; AAC44040.1; -; Genomic_DNA.
DR   AlphaFoldDB; P58997; -.
DR   BMRB; P58997; -.
DR   SMR; P58997; -.
DR   iPTMnet; P58997; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR007971; Bundlin.
DR   InterPro; IPR012902; N_methyl_site.
DR   InterPro; IPR045584; Pilin-like.
DR   Pfam; PF05307; Bundlin; 1.
DR   SUPFAM; SSF54523; SSF54523; 1.
DR   PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fimbrium; Membrane; Methylation;
KW   Plasmid; Transmembrane; Transmembrane helix.
FT   PROPEP          1..13
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT                   ECO:0000269|PubMed:1683004"
FT                   /id="PRO_0000024194"
FT   CHAIN           14..193
FT                   /note="Major structural subunit of bundle-forming pilus"
FT                   /id="PRO_0000024195"
FT   TRANSMEM        14..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         14
FT                   /note="N-methylleucine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT                   ECO:0000269|PubMed:1683004"
FT   DISULFID        129..179
FT                   /evidence="ECO:0000255"
FT   CONFLICT        14
FT                   /note="L -> M (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305|PubMed:1683004"
FT   CONFLICT        41
FT                   /note="S -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305|PubMed:1683004"
SQ   SEQUENCE   193 AA;  20300 MW;  2FCEC03E415FF026 CRC64;
     MVSKIMNKKY EKGLSLIESA MVLALAATVT AGVMFYYQSA SDSNKSQNAI SEVMSATSAI
     NGLYIGQTSY SGLDSTILLN TSAIPDNYKD TTNKKITNPF GGELNVGPAN NNTAFGYYLT
     LTRLDKAACV SLATLNLGTS AKGYGVNISS ENNITSFGNS ADQAAKSTAI TPAEAATACK
     NTDSTNKVTY FMK