Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. M.tuberculosis may use AcsA for both acetate and propionate assimilation. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Magnesium, but can also use calcium, manganese, nickel or zinc ions. Optimum pH is around 8. The enzyme is stable under neutral and alkaline conditions, while its activity decreases rapidly below pH 6.0. Optimum temperature is 37 degrees Celsius. It lost its activity rapidly below 25 degrees Celsius or above 45 degrees Celsius. Acetylated on Lys-617 by Pat in the presence of acetyl-CoA as an acetyl donor and ATP. Acetylation results in the inactivation of the enzyme. Deacetylation by the SIR2-homolog deacetylase CobB is required to activate the enzyme. Could be also autoacetylated on Lys-617 in the presence of acetate as an acetyl donor and ATP. Autoacetylation is effectively inhibited by CoA. If CoA is not available or the concentration of CoA is low in vivo, the enzyme can transfer acetyl group from AcAMP to itself, resulting in autoacetylation and inactivation. When CoA is available, the acetyl group is donated to CoA forming AcCoA (PubMed:21896569). Belongs to the ATP-dependent AMP-binding enzyme family.