BCR_ECOLI
ID BCR_ECOLI Reviewed; 396 AA.
AC P28246; Q2MAQ9;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 4.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Bicyclomycin resistance protein;
DE AltName: Full=Sulfonamide resistance protein;
GN Name=bcr; Synonyms=bicA, bicR, sur {ECO:0000303|PubMed:2694948}, suxA;
GN OrderedLocusNames=b2182, JW5363;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nichols B.P.;
RL Unpublished observations (FEB-1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-396.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=8486276; DOI=10.1016/0378-1119(93)90625-d;
RA Bentley J., Hyatt L.S., Ainley K., Parish J.H., Herbert R.B., White G.R.;
RT "Cloning and sequence analysis of an Escherichia coli gene conferring
RT bicyclomycin resistance.";
RL Gene 127:117-120(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION.
RX PubMed=2694948; DOI=10.1128/aac.33.12.2042;
RA Nichols B.P., Guay G.G.;
RT "Gene amplification contributes to sulfonamide resistance in Escherichia
RT coli.";
RL Antimicrob. Agents Chemother. 33:2042-2048(1989).
RN [7]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [8]
RP FUNCTION.
RC STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RX PubMed=20067529; DOI=10.1111/j.1574-6968.2009.01879.x;
RA Hayashi M., Tabata K., Yagasaki M., Yonetani Y.;
RT "Effect of multidrug-efflux transporter genes on dipeptide resistance and
RT overproduction in Escherichia coli.";
RL FEMS Microbiol. Lett. 304:12-19(2010).
CC -!- FUNCTION: Involved in sulfonamide (sulfathiazole) and bicyclomycin
CC resistance (PubMed:2694948). Probable membrane translocase. A
CC transporter able to export peptides. When overexpressed, allows cells
CC deleted for multiple peptidases (pepA, pepB, pepD and pepN) to grow in
CC the presence of dipeptides Ala-Gln or Gly-Tyr which otherwise inhibit
CC growth (PubMed:20067529). Cells overexpressing this protein have
CC decreased intracellular levels of Ala-Gln dipeptide, and in a system
CC that produces the Ala-Gln dipeptide overproduction of this protein
CC increases export of the dipeptide (PubMed:20067529).
CC {ECO:0000269|PubMed:2694948}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Bcr/CmlA
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16406.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA45230.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X63703; CAA45230.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00008; AAA16406.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75243.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76647.1; -; Genomic_DNA.
DR PIR; E64987; E64987.
DR RefSeq; NP_416687.1; NC_000913.3.
DR RefSeq; WP_000213361.1; NZ_SSZK01000027.1.
DR AlphaFoldDB; P28246; -.
DR SMR; P28246; -.
DR BioGRID; 4260471; 162.
DR STRING; 511145.b2182; -.
DR TCDB; 2.A.1.2.7; the major facilitator superfamily (mfs).
DR PaxDb; P28246; -.
DR PRIDE; P28246; -.
DR EnsemblBacteria; AAC75243; AAC75243; b2182.
DR EnsemblBacteria; BAE76647; BAE76647; BAE76647.
DR GeneID; 944808; -.
DR KEGG; ecj:JW5363; -.
DR KEGG; eco:b2182; -.
DR PATRIC; fig|1411691.4.peg.54; -.
DR EchoBASE; EB1390; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_47_0_6; -.
DR InParanoid; P28246; -.
DR OMA; YFFMLNI; -.
DR PhylomeDB; P28246; -.
DR BioCyc; EcoCyc:BCR-MON; -.
DR BioCyc; MetaCyc:BCR-MON; -.
DR PRO; PR:P28246; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0033229; F:cysteine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0033228; P:cysteine export across plasma membrane; IMP:EcoCyc.
DR GO; GO:0035442; P:dipeptide transmembrane transport; IMP:EcoCyc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:EcoCyc.
DR InterPro; IPR004812; Efflux_drug-R_Bcr/CmlA.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004734; Multidrug-R.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00880; 2_A_01_02; 1.
DR TIGRFAMs; TIGR00710; efflux_Bcr_CflA; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW Peptide transport; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..396
FT /note="Bicyclomycin resistance protein"
FT /id="PRO_0000173315"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..48
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..105
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..165
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..250
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..308
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..372
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT CONFLICT 99
FT /note="D -> V (in Ref. 2; CAA45230)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="V -> I (in Ref. 1 and 2; CAA45230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 43353 MW; D609AE35370E6A1D CRC64;
MTTRQHSSFA IVFILGLLAM LMPLSIDMYL PALPVISAQF GVPAGSTQMT LSTYILGFAL
GQLIYGPMAD SFGRKPVVLG GTLVFAAAAV ACALANTIDQ LIVMRFFHGL AAAAASVVIN
ALMRDIYPKE EFSRMMSFVM LVTTIAPLMA PIVGGWVLVW LSWHYIFWIL ALAAILASAM
IFFLIKETLP PERRQPFHIR TTIGNFAALF RHKRVLSYML ASGFSFAGMF SFLSAGPFVY
IEINHVAPEN FGYYFALNIV FLFVMTIFNS RFVRRIGALN MFRSGLWIQF IMAAWMVISA
LLGLGFWSLV VGVAAFVGCV SMVSSNAMAV ILDEFPHMAG TASSLAGTFR FGIGAIVGAL
LSLATFNSAW PMIWSIAFCA TSSILFCLYA SRPKKR
