ID   DRRB_MYCTO              Reviewed;         289 AA.
AC   P9WG22; L0TB30; P96206; Q7D6E7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Doxorubicin resistance ABC transporter permease protein DrrB;
GN   Name=drrB; OrderedLocusNames=MT3007;
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. Probably responsible for the translocation of
CC       the substrate across the membrane (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}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47334.1; -; Genomic_DNA.
DR   PIR; E70984; E70984.
DR   RefSeq; WP_003414848.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WG22; -.
DR   EnsemblBacteria; AAK47334; AAK47334; MT3007.
DR   GeneID; 45426925; -.
DR   KEGG; mtc:MT3007; -.
DR   PATRIC; fig|83331.31.peg.3247; -.
DR   HOGENOM; CLU_039483_2_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
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   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR000412; ABC_2_transport.
DR   InterPro; IPR004377; ABC_transpt_DrrB/DrrC.
DR   PIRSF; PIRSF006648; DrrB; 1.
DR   TIGRFAMs; TIGR00025; Mtu_efflux; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..289
FT                   /note="Doxorubicin resistance ABC transporter permease
FT                   protein DrrB"
FT                   /id="PRO_0000428437"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          47..282
FT                   /note="ABC transmembrane type-2"
SQ   SEQUENCE   289 AA;  31109 MW;  45ED403F53C54A34 CRC64;
     MSGPAIDASP ALTFNQSSAS IQQRRLSTGR QMWVLYRRFA APSLLNGEVL TTVGAPIIFM
     VGFYIPFAIP WNQFVGGASS GVASNLGQYI TPLVTLQAVS FAAIGSGFRA ATDSLLGVNR
     RFQSMPMAPL TPLLARVWVA VDRCFTGLVI SLVCGYVIGF RFHRGALYIV GFCLLVIAIG
     AVLSFAADLV GTVTRNPDAM LPLLSLPILI FGLLSIGLMP LKLFPHWIHP FVRNQPISQF
     VAALRALAGD TTKTASQVSW PVMAPTLTWL FAFVVILALS STIVLARRP