ATP synthase subunit c (mycobacteria) (AtpE)

ATP synthase subunit c is an essential part of the F₀ sector of ATP synthase in mycobacteria, forming a multi-copy ring (c-ring) within the cytoplasmic membrane that drives ATP production via rotary catalysis powered by the proton-motive force[1][2]. In Mycobacterium tuberculosis, the c subunit (commonly termed AtpE) forms the drug-binding site for bedaquiline, a first-in-class antitubercular agent. The subunit is directly involved in translocating protons across the membrane, which rotates the c-ring and drives conformational changes in the F₁ sector, thereby synthesizing ATP. As an essential membrane protein facilitating ATP generation, it is indispensable for mycobacterial survival, especially under hypoxic or persistent infection conditions[2][7]. Targeting subunit c has led to the development of highly potent antimycobacterial drugs, although resistance can emerge through mutation of the atpE gene[6].

Other names

AtpEc subunit of ATP synthasesubunit c (F₀ sector)

Inhibition of proton translocation by binding to subunit c, thereby blocking ATP synthesis