TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


3.A.1.105.1
Daunorubicin, doxorubicin etc. (multidrug resistance) exporter, DrrAB.  DrrB binds drugs with variable affinities and contains multiple drug binding sites. The two asymmetric nucleotide binding sites in DrrA have strikingly different binding affinities. Long-range conformational changes occur between DrrA and DrrB. The transduction pathway from the nucleotide-binding DrrA subunit to the substrate binding DrrB subunit includes the Q-loop and CREEM motifs in DrrA and the EAA-like motif in DrrB (Rahman and Kaur 2018).

Accession Number:P32010
Protein Name:DrrA
Length:330
Molecular Weight:35700.00
Species:Streptomyces peucetius [1950]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell membrane1 / Peripheral membrane protein2 / Cytoplasmic side3
Substrate daunorubicin, doxorubicin

Cross database links:

Pfam: PF00005   

Gene Ontology

GO:0009898 C:internal side of plasma membrane
GO:0005524 F:ATP binding
GO:0016887 F:ATPase activity
GO:0005525 F:GTP binding
GO:0046677 P:response to antibiotic
GO:0006810 P:transport

References (2)

[1] “A bacterial analog of the mdr gene of mammalian tumor cells is present in Streptomyces peucetius, the producer of daunorubicin and doxorubicin.”  Guilfoile P.G.et.al.   1924314
[2] “Expression and characterization of DrrA and DrrB proteins of Streptomyces peucetius in Escherichia coli: DrrA is an ATP binding protein.”  Kaur P.et.al.   9006006

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MNTQPTRAIE TSGLVKVYNG TRAVDGLDLN VPAGLVYGIL GPNGAGKSTT IRMLATLLRP 
61:	DGGTARVFGH DVTSEPDTVR RRISVTGQYA SVDEGLTGTE NLVMMGRLQG YSWARARERA 
121:	AELIDGFGLG DARDRLLKTY SGGMRRRLDI AASIVVTPDL LFLDEPTTGL DPRSRNQVWD 
181:	IVRALVDAGT TVLLTTQYLD EADQLADRIA VIDHGRVIAE GTTGELKSSL GSNVLRLRLH 
241:	DAQSRAEAER LLSAELGVTI HRDSDPTALS ARIDDPRQGM RALAELSRTH LEVRSFSLGQ 
301:	SSLDEVFLAL TGHPADDRST EEAAEEEKVA