ID   EBRB_BACAT              Reviewed;         117 AA.
AC   P0CW83; O31791; Q9R9H9;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Multidrug resistance protein EbrB;
GN   Name=ebrB;
OS   Bacillus atrophaeus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1452;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC   STRAIN=ATCC 9372 / DSM 675 / NBRC 13721 / NCIMB 8058 / NRS 1221A;
RX   PubMed=10735876; DOI=10.1128/jb.182.8.2307-2310.2000;
RA   Masaoka Y., Ueno Y., Morita Y., Kuroda T., Mizushima T., Tsuchiya T.;
RT   "A two-component multidrug efflux pump, EbrAB, in Bacillus subtilis.";
RL   J. Bacteriol. 182:2307-2310(2000).
CC   -!- FUNCTION: Part of a multidrug efflux pump. Confers resistance to
CC       cationic lipophilic dyes such as ethidium bromide, acriflavine,
CC       pyronine Y and safranin O. The efflux is probably coupled to an influx
CC       of protons. {ECO:0000269|PubMed:10735876}.
CC   -!- SUBUNIT: The efflux pump is composed of EbrA and EbrB.
CC       {ECO:0000305|PubMed:10735876}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the drug/metabolite transporter (DMT)
CC       superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family.
CC       EbrA/EbrB subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA88576.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB029306; BAA88576.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P0CW83; -.
DR   SMR; P0CW83; -.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR000390; Small_drug/metabolite_transptr.
DR   InterPro; IPR045324; Small_multidrug_res.
DR   PANTHER; PTHR30561; PTHR30561; 1.
DR   Pfam; PF00893; Multi_Drug_Res; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..117
FT                   /note="Multidrug resistance protein EbrB"
FT                   /id="PRO_0000408957"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   117 AA;  12256 MW;  5DECE8EBB16399C8 CRC64;
     MKGLLYLALA IVSEVFGSTM LKLSEGFTQA WPIGGVIAGF LSAFTFLSFS LKTIDLSSAY
     ATWSGVGTAL TAIVGFLLFG ETISLKGVFG LTLVIAGVVV LNQSKAPAKE KKQTVCE