Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS). This acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental changes. Autoinhibited and allosterically activated by 3,5-cyclic adenosine monophosphate (cAMP). An extensive conformational rearrangement relieves this autoinhibition by means of a substrate-mimicking lid that covers the protein-substrate binding surface. Homodimer.