Catalyzes the N-acetylation of S-(2-succino)cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine. Moreover, 2SC is a toxic compound in B.subtilis at high exogenous concentrations, and this enzyme relieves 2SC toxicity via N-acetylation. acetyl-CoA + S-(2-succino)-L-cysteine = CoA + H(+) + N-acetyl-S-(2-succino)-L-cysteine kcat is 9.5 sec(-1). Amino-acid biosynthesis; L-cysteine biosynthesis. Cells lacking this gene almost lose the ability to grow on 2SC as the sulfur source but are still able to grow on sulfate. Moreover, in contrast to wild type, they highly accumulate 2SC when grown on fumarate as the sulfur source. Addition of 2SC causes growth inhibition of the deletion mutant but not the wild type grown on sulfate as the sulfur source. Fumarate mediated succination of thiols increases in certain tumors and in response to glucotoxicity associated with diabetes. Therefore, S-(2-succino)-adducts such as S-(2-succino)cysteine (2SC) are considered oncometabolites and biomarkers for human disease. The demonstration of a metabolic disposal route for a S-(2-succino)-compound paves the way toward the identification of corresponding pathways in other species. Belongs to the acetyltransferase family.