Modulation of the bacterial CobB sirtuin deacylase activity by N-terminal acetylation

Significance N-terminal protein acetylation is poorly understood in bacteria. Herein, we report the identification of an Nα acetyltransferase (NAT) that modulates the activity of a sirtuin deacylase in a human pathogen. This is significant because the alluded enzyme (named N -acyltransferase A [NatA], formerly YiaC) is a prokaryotic non-Rim–type NAT, and N - terminal acetylation of a bacterial sirtuin has not been reported. Also significant is the fact that NatA affects the metabolism of acetate, a short-chain fatty acid known to play an important role in pathogenesis in the human gut.