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Daunorubicin/doxorubicin resistance ATP-binding protein DrrA (EC 3.6.3.-)

 DRRA_STRPE              Reviewed;         330 AA.
P32010;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
12-APR-2017, entry version 78.
RecName: Full=Daunorubicin/doxorubicin resistance ATP-binding protein DrrA;
EC=3.6.3.-;
Name=drrA;
Streptomyces peucetius.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1950;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN RESISTANCE.
STRAIN=ATCC 29050 / DSM 40754 / JCM 9920 / NBRC 100596 / NCIMB 10972;
PubMed=1924314; DOI=10.1073/pnas.88.19.8553;
Guilfoile P.G., Hutchinson C.R.;
"A bacterial analog of the mdr gene of mammalian tumor cells is
present in Streptomyces peucetius, the producer of daunorubicin and
doxorubicin.";
Proc. Natl. Acad. Sci. U.S.A. 88:8553-8557(1991).
[2]
FUNCTION, ATP-BINDING, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=9006006; DOI=10.1128/jb.179.3.569-575.1997;
Kaur P.;
"Expression and characterization of DrrA and DrrB proteins of
Streptomyces peucetius in Escherichia coli: DrrA is an ATP binding
protein.";
J. Bacteriol. 179:569-575(1997).
-!- FUNCTION: Part of the ABC transporter complex DrrAB involved in
daunorubicin and doxorubicin resistance. Responsible for energy
coupling to the transport system. Binds ATP or GTP.
{ECO:0000269|PubMed:1924314, ECO:0000269|PubMed:9006006}.
-!- SUBUNIT: The complex is composed of two ATP-binding proteins
(DrrA) and two transmembrane proteins (DrrB).
{ECO:0000305|PubMed:9006006}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9006006};
Peripheral membrane protein {ECO:0000269|PubMed:9006006};
Cytoplasmic side {ECO:0000269|PubMed:9006006}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. Drug
exporter-1 (DrugE1) (TC 3.A.1.105) family. {ECO:0000305}.
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EMBL; M73758; AAA74717.1; -; Genomic_DNA.
PIR; S27707; S27707.
ProteinModelPortal; P32010; -.
SMR; P32010; -.
TCDB; 3.A.1.105.1; the atp-binding cassette (abc) superfamily.
PRIDE; P32010; -.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0016887; F:ATPase activity; IEA:InterPro.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0043215; P:daunorubicin transport; IEA:InterPro.
GO; GO:1900753; P:doxorubicin transport; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR005894; DrrA.
InterPro; IPR025302; DUF4162.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00005; ABC_tran; 1.
Pfam; PF13732; DUF4162; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01188; drrA; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
Antibiotic resistance; ATP-binding; Cell membrane; Hydrolase;
Membrane; Nucleotide-binding; Transport.
CHAIN 1 330 Daunorubicin/doxorubicin resistance ATP-
binding protein DrrA.
/FTId=PRO_0000092319.
DOMAIN 9 239 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 41 48 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
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


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