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).
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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 |
---|
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