2.A.1.3.78 Drug resistance pump, EfpA of 530 aas and 14 TMSs. May function with IniABC (see TC# 9.B.282), shown to influence resistance to several drugs (Colangeli et al. 2007). CryoEM structures of the essential drug efflux pump EfpA from Mycobacterium tuberculosis reveal the mechanisms of substrate transport and small-molecule inhibition (Wang et al. 2024). It exists in an outward-open conformation, either bound to three endogenous lipids or
the inhibitor BRD-8000.3. Three lipids inside EfpA span from the inner
leaflet to the outer leaflet of the membrane. BRD-8000.3 occupies one
lipid site at the level of inner membrane leaflet, competitively
inhibiting lipid binding. EfpA resembles the related lysophospholipid
transporter MFSD2A (TC# 2.A.2.3.8) in both overall structure and lipid binding sites and
may function as a lipid flippase (Wang et al. 2024).
|
Accession Number: | P9WJY5 |
Protein Name: | Uncharacterized MFS-type transporter EfpA |
Length: | 530 |
Molecular Weight: | 55580.00 |
Species: | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) [83332] |
Number of TMSs: | 14 |
Location1 / Topology2 / Orientation3: |
Cell membrane1 / Multi-pass membrane protein2 |
Substrate |
|
---|
1: MTALNDTERA VRNWTAGRPH RPAPMRPPRS EETASERPSR YYPTWLPSRS FIAAVIAIGG
61: MQLLATMDST VAIVALPKIQ NELSLSDAGR SWVITAYVLT FGGLMLLGGR LGDTIGRKRT
121: FIVGVALFTI SSVLCAVAWD EATLVIARLS QGVGSAIASP TGLALVATTF PKGPARNAAT
181: AVFAAMTAIG SVMGLVVGGA LTEVSWRWAF LVNVPIGLVM IYLARTALRE TNKERMKLDA
241: TGAILATLAC TAAVFAFSIG PEKGWMSGIT IGSGLVALAA AVAFVIVERT AENPVVPFHL
301: FRDRNRLVTF SAILLAGGVM FSLTVCIGLY VQDILGYSAL RAGVGFIPFV IAMGIGLGVS
361: SQLVSRFSPR VLTIGGGYLL FGAMLYGSFF MHRGVPYFPN LVMPIVVGGI GIGMAVVPLT
421: LSAIAGVGFD QIGPVSAIAL MLQSLGGPLV LAVIQAVITS RTLYLGGTTG PVKFMNDVQL
481: AALDHAYTYG LLWVAGAAII VGGMALFIGY TPQQVAHAQE VKEAIDAGEL