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Here, we report that SrtA can mediate the efficient and irreversible ligation of a protein\/peptide containing a C\u2010terminal thioester with another protein\/peptide bearing an N\u2010terminal Gly, with broad tolerance for a wide variety of LPxT\u2010derived sequences. This strategy, the thioester\u2010assisted SrtA\u2010mediated ligation, enabled the expedient preparation of proteins bearing various N\u2010 or C\u2010terminal labels, including post\u2010translationally modified proteins such as the Ser139\u2010phosphorylated histone H2AX and Lys9\u2010methylated histone H3, with less dependence on the LPxTG motif. 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