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3.A.1.117.3
Multidrug resistance homodimeric efflux pump, BmrA (YvcC) of 589 aas (Dalmas et al. 2005).  The low resolution cryo-electron microscopy reconstitution suggests large conformational changes occur during it's catalytic cycle (Fribourg et al. 2014). Backbone NMR assignments of the nucleotide binding domain of BmrA in the post-hydrolysis state have been determined (Pérez Carrillo et al. 2022). The protein is homodimeric, and it's unfolding and themodynamic stability have been studied (Oepen et al. 2023).

Accession Number:O06967
Protein Name:Multidrug resistance ABC transporter ATP-binding/permease protein BmrA
Length:589
Molecular Weight:64519.00
Species:Bacillus subtilis (strain 168) [224308]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate drug

Cross database links:

Structure:
6R72   6R81     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MPTKKQKSKS KLKPFFALVR RTNPSYGKLA FALALSVVTT LVSLLIPLLT KQLVDGFSMS 
61:	NLSGTQIGLI ALVFFVQAGL SAYATYALNY NGQKIISGLR ELLWKKLIKL PVSYFDTNAS 
121:	GETVSRVTND TMVVKELITT HISGFITGII SVIGSLTILF IMNWKLTLLV LVVVPLAALI 
181:	LVPIGRKMFS ISRETQDETA RFTGLLNQIL PEIRLVKASN AEDVEYGRGK MGISSLFKLG 
241:	VREAKVQSLV GPLISLVLMA ALVAVIGYGG MQVSSGELTA GALVAFILYL FQIIMPMGQI 
301:	TTFFTQLQKS IGATERMIEI LAEEEEDTVT GKQIENAHLP IQLDRVSFGY KPDQLILKEV 
361:	SAVIEAGKVT AIVGPSGGGK TTLFKLLERF YSPTAGTIRL GDEPVDTYSL ESWREHIGYV 
421:	SQESPLMSGT IRENICYGLE RDVTDAEIEK AAEMAYALNF IKELPNQFDT EVGERGIMLS 
481:	GGQRQRIAIA RALLRNPSIL MLDEATSSLD SQSEKSVQQA LEVLMEGRTT IVIAHRLSTV 
541:	VDADQLLFVE KGEITGRGTH HELMASHGLY RDFAEQQLKM NADLENKAG