DRRA_MYCTU
ID DRRA_MYCTU Reviewed; 331 AA.
AC P9WQL9; 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 42.
DE RecName: Full=Doxorubicin resistance ATP-binding protein DrrA;
DE EC=7.6.2.-;
GN Name=drrA; OrderedLocusNames=Rv2936;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION IN DOXORUBICIN RESISTANCE, ATP-BINDING, ACTIVITY REGULATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12057006; DOI=10.1042/bj20020615;
RA Choudhuri B.S., Bhakta S., Barik R., Basu J., Kundu M., Chakrabarti P.;
RT "Overexpression and functional characterization of an ABC (ATP-binding
RT cassette) transporter encoded by the genes drrA and drrB of Mycobacterium
RT tuberculosis.";
RL Biochem. J. 367:279-285(2002).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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. {ECO:0000269|PubMed:12057006}.
CC -!- ACTIVITY REGULATION: Inhibited by reserpine.
CC {ECO:0000269|PubMed:12057006}.
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:0000305|PubMed:12057006};
CC Peripheral membrane protein {ECO:0000305|PubMed:12057006}; Cytoplasmic
CC side {ECO:0000305|PubMed:12057006}.
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; AL123456; CCP45739.1; -; Genomic_DNA.
DR PIR; D70984; D70984.
DR RefSeq; NP_217452.1; NC_000962.3.
DR RefSeq; WP_003901496.1; NZ_NVQJ01000015.1.
DR AlphaFoldDB; P9WQL9; -.
DR SMR; P9WQL9; -.
DR STRING; 83332.Rv2936; -.
DR PaxDb; P9WQL9; -.
DR DNASU; 888168; -.
DR GeneID; 888168; -.
DR KEGG; mtu:Rv2936; -.
DR TubercuList; Rv2936; -.
DR eggNOG; COG1131; Bacteria.
DR OMA; ISMPAPD; -.
DR PhylomeDB; P9WQL9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0043215; P:daunorubicin transport; IEA:InterPro.
DR GO; GO:1900753; P:doxorubicin transport; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IMP:MTBBASE.
DR GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Antibiotic resistance; ATP-binding; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..331
FT /note="Doxorubicin resistance ATP-binding protein DrrA"
FT /id="PRO_0000393225"
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
