ID   DRRA_MYCTO              Reviewed;         331 AA.
AC   P9WQL8; L0TCP0; P96205; Q7D6E8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Doxorubicin resistance ATP-binding protein DrrA;
DE            EC=7.6.2.-;
GN   Name=drrA; OrderedLocusNames=MT3006;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Part of the ABC transporter complex DrrABC involved in
CC       doxorubicin resistance. Responsible for energy coupling to the
CC       transport system. Binds ATP (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (DrrA) and
CC       two transmembrane proteins (DrrB and DrrC). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
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; AE000516; AAK47333.1; -; Genomic_DNA.
DR   PIR; D70984; D70984.
DR   RefSeq; WP_003901496.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQL8; -.
DR   SMR; P9WQL8; -.
DR   EnsemblBacteria; AAK47333; AAK47333; MT3006.
DR   KEGG; mtc:MT3006; -.
DR   PATRIC; fig|83331.31.peg.3246; -.
DR   HOGENOM; CLU_000604_1_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 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   3: Inferred from homology;
KW   Antibiotic resistance; ATP-binding; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..331
FT                   /note="Doxorubicin resistance ATP-binding protein DrrA"
FT                   /id="PRO_0000426753"
FT   DOMAIN          8..240
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   331 AA;  35818 MW;  9102BCEFD6419046 CRC64;
     MRNDDMAVVV NGVRKTYGKG KIVALDDVSF KVRRGEVIGL LGPNGAGKTT MVDILSTLTR
     PDAGSAIIAG YDVVSEPAGV RRSIMVTGQQ VAVDDALSGE QNLVLFGRLW GLSKSAARKR
     AAELLEQFSL VHAGKRRVGT YSGGMRRRID IACGLVVQPQ VAFLDEPTTG LDPRSRQAIW
     DLVASFKKLG IATLLTTQYL EEADALSDRI ILIDHGIIIA EGTANELKHR AGDTFCEIVP
     RDLKDLDAIV AALGSLLPEH HRAMLTPDSD RITMPAPDGI RMLVEAARRI DEARIELADI
     ALRRPSLDHV FLAMTTDPTE SLTHLVSGSA R