ID   DRRB_STRPE              Reviewed;         283 AA.
AC   P32011;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Daunorubicin/doxorubicin resistance ABC transporter permease protein DrrB;
GN   Name=drrB;
OS   Streptomyces peucetius.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN RESISTANCE.
RC   STRAIN=ATCC 29050 / DSM 40754 / JCM 9920 / NBRC 100596 / NCIMB 10972;
RX   PubMed=1924314; DOI=10.1073/pnas.88.19.8553;
RA   Guilfoile P.G., Hutchinson C.R.;
RT   "A bacterial analog of the mdr gene of mammalian tumor cells is present in
RT   Streptomyces peucetius, the producer of daunorubicin and doxorubicin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:8553-8557(1991).
RN   [2]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=9006006; DOI=10.1128/jb.179.3.569-575.1997;
RA   Kaur P.;
RT   "Expression and characterization of DrrA and DrrB proteins of Streptomyces
RT   peucetius in Escherichia coli: DrrA is an ATP binding protein.";
RL   J. Bacteriol. 179:569-575(1997).
RN   [3]
RP   TOPOLOGY.
RX   PubMed=15090538; DOI=10.1074/jbc.m402898200;
RA   Gandlur S.M., Wei L., Levine J., Russell J., Kaur P.;
RT   "Membrane topology of the DrrB protein of the doxorubicin transporter of
RT   Streptomyces peucetius.";
RL   J. Biol. Chem. 279:27799-27806(2004).
CC   -!- FUNCTION: Part of the ABC transporter complex DrrAB involved in
CC       daunorubicin and doxorubicin resistance. Probably responsible for the
CC       translocation of the substrate across the membrane.
CC       {ECO:0000269|PubMed:1924314, ECO:0000269|PubMed:9006006}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (DrrA) and
CC       two transmembrane proteins (DrrB). {ECO:0000305|PubMed:9006006}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9006006};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:9006006}.
CC   -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family.
CC       {ECO:0000305}.
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DR   EMBL; M73758; AAA74718.1; -; Genomic_DNA.
DR   PIR; S27708; S27708.
DR   AlphaFoldDB; P32011; -.
DR   TCDB; 3.A.1.105.1; the atp-binding cassette (abc) superfamily.
DR   KEGG; ag:AAA74718; -.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR013525; ABC_2_trans.
DR   InterPro; IPR000412; ABC_2_transport.
DR   Pfam; PF01061; ABC2_membrane; 1.
DR   PIRSF; PIRSF006648; DrrB; 1.
DR   PROSITE; PS51012; ABC_TM2; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..283
FT                   /note="Daunorubicin/doxorubicin resistance ABC transporter
FT                   permease protein DrrB"
FT                   /id="PRO_0000182981"
FT   TOPO_DOM        1..53
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..87
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..119
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..169
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..199
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..262
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..283
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          53..280
FT                   /note="ABC transmembrane type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
SQ   SEQUENCE   283 AA;  30614 MW;  EC42F07A4D15C07A CRC64;
     MTTSPGTVES TTPVSGQLRT VLSAGERPAR ATAVSATLTH LWRAMMAFKH FPVQLIDIVL
     MPLIFLLMFT YLFGGAFADS TEEYLQFYLP GVTVQAVVMM TVYTGTSLNT DIHKGVFDRF
     RTLPFWQPAT LAGSLLGDVL RYVVALATTV SLGLLLGFRA DGGFLGVVGA MLVLIVFGFS
     VSWIFAALGV VASEPERVSG TSMIVLYPLL FMSNIFVMPE TMPGWMQAIV DANPMSHAAT
     ASRELMHGTA GFWDVGLVLC VSAGLVAVFA PLTMRLYRNK NAH