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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

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FASTA formatted sequence
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