Involved in the translocation of an unknown substrate across the membrane. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for virulence. Function is positively regulated by phosphorylation. Homodimer (Probable). Interacts with PknF. In Rv1747 the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused. The two FHA domains are required for phosphorylation by PknF. Phosphorylated by PknF. Can probably be phosphorylated in vivo by other kinases when PknF is missing. Disruption results in a growth defect in macrophage and mouse infections. In the central section; belongs to the ABC transporter superfamily. In the C-terminal section; belongs to the ABC-2 integral membrane protein family.