ID   DRRA_STRPE              Reviewed;         330 AA.
AC   P32010;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Daunorubicin/doxorubicin resistance ATP-binding protein DrrA;
DE            EC=7.6.2.-;
GN   Name=drrA;
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, ATP-BINDING, 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).
CC   -!- FUNCTION: Part of the ABC transporter complex DrrAB involved in
CC       daunorubicin and doxorubicin resistance. Responsible for energy
CC       coupling to the transport system. Binds ATP or GTP.
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       Peripheral membrane protein {ECO:0000269|PubMed:9006006}; Cytoplasmic
CC       side {ECO:0000269|PubMed:9006006}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Drug exporter-1
CC       (DrugE1) (TC 3.A.1.105) family. {ECO:0000305}.
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DR   EMBL; M73758; AAA74717.1; -; Genomic_DNA.
DR   PIR; S27707; S27707.
DR   AlphaFoldDB; P32010; -.
DR   SMR; P32010; -.
DR   TCDB; 3.A.1.105.1; the atp-binding cassette (abc) superfamily.
DR   KEGG; ag:AAA74717; -.
DR   BRENDA; 7.6.2.2; 6073.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0043215; P:daunorubicin transport; IEA:InterPro.
DR   GO; GO:1900753; P:doxorubicin transport; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR005894; DrrA.
DR   InterPro; IPR025302; DUF4162.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF13732; DUF4162; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01188; drrA; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; ATP-binding; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..330
FT                   /note="Daunorubicin/doxorubicin resistance ATP-binding
FT                   protein DrrA"
FT                   /id="PRO_0000092319"
FT   DOMAIN          9..239
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   330 AA;  35700 MW;  582D66C90D54E6B9 CRC64;
     MNTQPTRAIE TSGLVKVYNG TRAVDGLDLN VPAGLVYGIL GPNGAGKSTT IRMLATLLRP
     DGGTARVFGH DVTSEPDTVR RRISVTGQYA SVDEGLTGTE NLVMMGRLQG YSWARARERA
     AELIDGFGLG DARDRLLKTY SGGMRRRLDI AASIVVTPDL LFLDEPTTGL DPRSRNQVWD
     IVRALVDAGT TVLLTTQYLD EADQLADRIA VIDHGRVIAE GTTGELKSSL GSNVLRLRLH
     DAQSRAEAER LLSAELGVTI HRDSDPTALS ARIDDPRQGM RALAELSRTH LEVRSFSLGQ
     SSLDEVFLAL TGHPADDRST EEAAEEEKVA