BFPA_ECO27
ID BFPA_ECO27 Reviewed; 193 AA.
AC P33553; B7UTD1; Q798R3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Major structural subunit of bundle-forming pilus;
DE AltName: Full=Bundle-forming pilin;
DE Short=BFP;
DE Short=Bundlin;
DE Flags: Precursor;
GN Name=bfpA; OrderedLocusNames=E2348_P1_003;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OG Plasmid pMAR2.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1362446; DOI=10.1111/j.1365-2958.1992.tb02210.x;
RA Donnenberg M.S., Giron J.A., Nataro J.P., Kaper J.B.;
RT "A plasmid-encoded type IV fimbrial gene of enteropathogenic Escherichia
RT coli associated with localized adherence.";
RL Mol. Microbiol. 6:3427-3437(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8733231; DOI=10.1111/j.1365-2958.1996.tb02620.x;
RA Stone K.D., Zhang H., Carlson L.K., Donnenberg M.S.;
RT "A cluster of fourteen genes from enteropathogenic Escherichia coli is
RT sufficient for the biogenesis of a type IV pilus.";
RL Mol. Microbiol. 20:325-337(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11083828; DOI=10.1128/iai.68.12.7028-7038.2000;
RA Blank T.E., Zhong H., Bell A.L., Whittam T.S., Donnenberg M.S.;
RT "Molecular variation among type IV pilin (bfpA) genes from diverse
RT enteropathogenic Escherichia coli strains.";
RL Infect. Immun. 68:7028-7038(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
RN [5]
RP PROTEIN SEQUENCE OF 14-41, AND METHYLATION AT LEU-14.
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).
RN [6]
RP FUNCTION.
RC STRAIN=B171;
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 [7]
RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=B171-8;
RX PubMed=9641917; DOI=10.1126/science.280.5372.2114;
RA Bieber D., Ramer S.W., Wu C.Y., Murray W.J., Tobe T., Fernandez R.,
RA Schoolnik G.K.;
RT "Type IV pili, transient bacterial aggregates, and virulence of
RT enteropathogenic Escherichia coli.";
RL Science 280:2114-2118(1998).
RN [8] {ECO:0007744|PDB:1ZWT}
RP STRUCTURE BY NMR OF 38-193, AND DISULFIDE BOND.
RX PubMed=16172128; DOI=10.1074/jbc.m508099200;
RA Ramboarina S., Fernandes P.J., Daniell S., Islam S., Simpson P.,
RA Frankel G., Booy F., Donnenberg M.S., Matthews S.;
RT "Structure of the bundle-forming pilus from enteropathogenic Escherichia
RT coli.";
RL J. Biol. Chem. 280:40252-40260(2005).
CC -!- FUNCTION: Major component of type IV bundle-forming pili (BFP) that
CC plays a role in adherence to host cells and virulence.
CC {ECO:0000269|PubMed:8096320, ECO:0000269|PubMed:9641917}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Fimbrium. Membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants cause significantly less
CC diarrhea in volonteers. {ECO:0000269|PubMed:9641917}.
CC -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.5; Type=Miscellaneous discrepancy; Note=The modified residue is misidentified as methionine.; Evidence={ECO:0000305|PubMed:1683004};
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DR EMBL; Z12295; CAA78167.1; -; Genomic_DNA.
DR EMBL; Z68186; CAA92326.1; -; Genomic_DNA.
DR EMBL; AF304474; AAG16262.1; -; Genomic_DNA.
DR EMBL; AF304480; AAG16268.1; -; Genomic_DNA.
DR EMBL; FM180569; CAS07439.1; -; Genomic_DNA.
DR PIR; S70966; S70966.
DR RefSeq; WP_000253757.1; NC_011603.1.
DR RefSeq; YP_001965379.1; NC_010862.1.
DR PDB; 1ZWT; NMR; -; A=38-193.
DR PDBsum; 1ZWT; -.
DR AlphaFoldDB; P33553; -.
DR BMRB; P33553; -.
DR SMR; P33553; -.
DR iPTMnet; P33553; -.
DR EnsemblBacteria; CAS07439; CAS07439; E2348_P1_003.
DR KEGG; ecg:E2348_P1_003; -.
DR HOGENOM; CLU_1376315_0_0_6; -.
DR OMA; ATACKNT; -.
DR EvolutionaryTrace; P33553; -.
DR Proteomes; UP000008205; Plasmid pMAR2.
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 3D-structure; Direct protein sequencing; Disulfide bond; Fimbrium;
KW Membrane; Methylation; Plasmid; Transmembrane; Transmembrane helix.
FT PROPEP 1..13
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:1683004"
FT /id="PRO_0000024196"
FT CHAIN 14..193
FT /note="Major structural subunit of bundle-forming pilus"
FT /id="PRO_0000024197"
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:0000269|PubMed:16172128,
FT ECO:0007744|PDB:1ZWT"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1ZWT"
FT HELIX 44..64
FT /evidence="ECO:0007829|PDB:1ZWT"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:1ZWT"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:1ZWT"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1ZWT"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1ZWT"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1ZWT"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1ZWT"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1ZWT"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1ZWT"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1ZWT"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:1ZWT"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:1ZWT"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:1ZWT"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:1ZWT"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1ZWT"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1ZWT"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:1ZWT"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:1ZWT"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1ZWT"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1ZWT"
SQ SEQUENCE 193 AA; 20270 MW; 2FCEC02E101AF426 CRC64;
MVSKIMNKKY EKGLSLIESA MVLALAATVT AGVMFYYQSA SDSNKSQNAI SEVMSATSAI
NGLYIGQTSY SGLDSTILLN TSAIPDNYKD TTNKKITNPF GGELNVGPAN NNTAFGYYLT
LTRLDKAACV SLATLNLGTS AKGYGVNISG ENNITSFGNS ADQAAKSTAI TPAEAATACK
NTDSTNKVTY FMK
