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Nα-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nα-acetyltransferases (NATs). Although present in all three domains of life, it is little understood in bacteria. The functional grouping of NATs into six types NatA - NatF, in eukaryotes is based on subunit requirements and stringent substrate specificities. Bacterial orthologs are phylogenetically divergent from eukaryotic NATs, and only a couple of them are characterized biochemically. Accordingly, not much is known about their substrate specificities.  Rv3420c  of  Mycobacterium tuberculosis  is a NAT ortholog coding for RimI Mtb . Using  in vitro  peptide-based enzyme assays and mass-spectrometry methods, we provide evidence that RimI Mtb  is a protein Nα-acetyltransferase of relaxed substrate specificity mimicking substrate specificities of eukaryotic NatA, NatC and most competently that of NatE. Also, hitherto unknown acetylation of residues namely, Asp, Glu, Tyr and Leu by a bacterial NAT (RimI Mtb ) is elucidated,  in vitro . Based on  in vivo  acetylation status,  in vitro  assay results and genetic context, a plausible cellular substrate for RimI Mtb  is proposed.

Biochemical evidence for relaxed substrate specificity of Nα-acetyltransferase (Rv3420c/rimI) of Mycobacterium tuberculosis