BCRB_ENTFL
ID BCRB_ENTFL Reviewed; 249 AA.
AC Q5WNX1;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Bacitracin transport permease protein BcrB {ECO:0000305};
GN Name=bcrB {ECO:0000303|PubMed:15388429};
GN ORFNames=BHU49_14280 {ECO:0000312|EMBL:OGX76143.1};
OS Enterococcus faecalis (Streptococcus faecalis).
OG Plasmid pJM01.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1351;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=AR01/DGVS;
RX PubMed=15388429; DOI=10.1128/aac.48.10.3743-3748.2004;
RA Manson J.M., Keis S., Smith J.M.B., Cook G.M.;
RT "Acquired bacitracin resistance in Enterococcus faecalis is mediated by an
RT ABC transporter and a novel regulatory protein, BcrR.";
RL Antimicrob. Agents Chemother. 48:3743-3748(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Enfs51;
RA Thong K.L., Tan S.C.;
RT "Comparative genome analysis of Enterococcus faecalis.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION.
RC STRAIN=AR01/DGVS;
RX PubMed=18227063; DOI=10.1074/jbc.m709503200;
RA Gauntlett J.C., Gebhard S., Keis S., Manson J.M., Pos K.M., Cook G.M.;
RT "Molecular analysis of BcrR, a membrane-bound bacitracin sensor and DNA-
RT binding protein from Enterococcus faecalis.";
RL J. Biol. Chem. 283:8591-8600(2008).
CC -!- FUNCTION: Essential for high-level bacitracin resistance
CC (PubMed:15388429). Part of the ABC transporter complex BcrAB. Probably
CC responsible for the translocation of the substrate across the membrane
CC (Probable). {ECO:0000269|PubMed:15388429, ECO:0000305|PubMed:15388429}.
CC -!- SUBUNIT: The complex is probably composed of two ATP-binding proteins
CC (BcrA) and two transmembrane proteins (BcrB). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Transcription is activated by the regulatory protein BcrR in
CC the presence of bacitracin. {ECO:0000269|PubMed:15388429,
CC ECO:0000269|PubMed:18227063}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant is sensitive to bacitracin.
CC {ECO:0000269|PubMed:15388429}.
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DR EMBL; AY496968; AAS78450.1; -; Genomic_DNA.
DR EMBL; MJEK01000021; OGX76143.1; -; Genomic_DNA.
DR RefSeq; WP_002367750.1; NZ_VWNQ01000021.1.
DR AlphaFoldDB; Q5WNX1; -.
DR SMR; Q5WNX1; -.
DR EnsemblBacteria; OGX76143; OGX76143; BHU49_14280.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Antibiotic resistance; Cell membrane; Membrane; Plasmid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..249
FT /note="Bacitracin transport permease protein BcrB"
FT /id="PRO_0000447367"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 249 AA; 27788 MW; 1A36D0AF3717CF49 CRC64;
MLNLISCELS KLKRSKMVLI SVAGVLSTPL LMLIEALQTH FDKPEIIFTL SDIYSDSVLY
IMLLVNMMIY VAIAAYLYSR EYTENTLKTI LPIPISRTKL LIGKFCTLLL WIVMLTLVTW
AGIFIVCGLY HVVFTLEGYS LLVAISWLPK FLFGGILMFL TTSPFVFIAF KTKGFVAPVI
ASAVIVMGSV ALSNQELGAL YPWTATFFLI DGRIESTGYP LALAIGIIIL VSAVGFFMTF
HHFKKEDLK