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).