BFPB_ECO11
ID BFPB_ECO11 Reviewed; 552 AA.
AC Q9S142; Q46777;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Outer membrane lipoprotein BfpB;
DE AltName: Full=Bundle-forming pilus B;
DE Flags: Precursor;
GN Name=bfpB;
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=8626330; DOI=10.1128/jb.178.9.2613-2628.1996;
RA Sohel I., Puente J.L., Ramer S.W., Bieber D., Wu C.-Y., Schoolnik G.K.;
RT "Enteropathogenic Escherichia coli: identification of a gene cluster coding
RT for bundle-forming pilus morphogenesis.";
RL J. Bacteriol. 178:2613-2628(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O111:H- / B171 / EPEC;
RX PubMed=10496929; DOI=10.1128/iai.67.10.5455-5462.1999;
RA Tobe T., Hayashi T., Han C.-G., Schoolnik G.K., Ohtsubo E., Sasakawa C.;
RT "Complete DNA sequence and structural analysis of the enteropathogenic
RT Escherichia coli adherence factor plasmid.";
RL Infect. Immun. 67:5455-5462(1999).
RN [3]
RP CHARACTERIZATION.
RC STRAIN=O111:H- / B171 / EPEC;
RX PubMed=8932312; DOI=10.1128/jb.178.22.6555-6563.1996;
RA Ramer S.W., Bieber D., Schoolnik G.K.;
RT "BfpB, an outer membrane lipoprotein required for the biogenesis of bundle-
RT forming pili in enteropathogenic Escherichia coli.";
RL J. Bacteriol. 178:6555-6563(1996).
CC -!- FUNCTION: Is absolutely required for pilus biogenesis, and for EPEC
CC localized adherence and autoaggregation. Acts at a step in the BFP
CC biogenic pathway after production and processing of the structural
CC pilus subunit BfpA.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor.
CC -!- INDUCTION: During exponential-phase growth; repressed by ammonium.
CC -!- SIMILARITY: Belongs to the bacterial secretin family. {ECO:0000305}.
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DR EMBL; U27184; AAC44041.1; -; Genomic_DNA.
DR EMBL; AB024946; BAA84840.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S142; -.
DR TCDB; 1.B.22.7.1; the outer bacterial membrane secretin (secretin) family.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009297; P:pilus assembly; IEA:InterPro.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR InterPro; IPR011514; Secretin_N_2.
DR InterPro; IPR004846; T2SS/T3SS.
DR Pfam; PF00263; Secretin; 1.
DR Pfam; PF07655; Secretin_N_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Fimbrium biogenesis; Lipoprotein; Membrane; Palmitate;
KW Plasmid; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000305"
FT CHAIN 18..552
FT /note="Outer membrane lipoprotein BfpB"
FT /id="PRO_0000020806"
FT REGION 218..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 332..335
FT /note="LLKH -> FVND (in Ref. 1; AAC44041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 58372 MW; F8CAE36171DCA956 CRC64;
MKLGRYSLFL LCPLLASCSG NGFYKDNLGV IDKNILHADT SLLKSKNKEH YKSSDMVSKT
DSIYIGNSSF QTYHGEPLPG KLEGVHGIIL RSSTPLGFDE VLSMIQDSSG IPIVKHTTKD
VISGGVSSKS LAATVAEKMN SATGGKSTDQ FDHLLLEVSS EHQLMDVNYQ GALSTFLDKV
AANYNLYWTY ESGRIAFSNE ETKRFSISIL PGGKYTSKNS ISSDSNSSSG SSGSSGSSSS
DSGAELKFDS DVDFWKDIEN SIKLILGSDG SYSISTSTSS VIVRTSSANM KKINEYINTL
NAQLERQVTI DVAIYNVTTT DSSDLAMSLE ALLKHNGGVL GSVSTSNFAA TSGTPSFTGY
LNGNGDSSNQ VLLNLLAEKG KVSVVTSASV TTMSGQPVPL KVGNDRTYVS EIGTVLSQSS
TSTTASTSTV TSGFLMNLLP QVADDGNILL QYGVTLSELV GSNNGFDQAT VNGTVIQLPN
VDSTTFVQSS MLRNGNTLVL AGYEKKRNES VDQGVGTTSF KLLGGALNGS ASRTVTVICI
TPRIIDLKAS GE