Update publication information. The antibiotics resistance of Edwardsiella tarda is prevailing, seeking a novel antimicrobial strategies extremely urgent. Lysine acylation has been proved to play important role on the bacterial physiological function while its role on bacterial antibiotics resistance mechanism still largely unclear. In this study, we investigated the lysine acetylation and succinylation profiles of E. tarda stain EIB202 using affinity antibody purification combined with LC MS/MS. A total of 1511 lysine-acetylation sites were identified on 589 proteins, and 2346 lysine-succinylation sites were further identified on 692 proteins of this pathogen. Further bioinformatics analysis showed that both PTMs prefer to enrich in TCA cycle, pyruvate metabolism. biosynthesis, and carbon metabolism. Besides, 948 peptides of 437 proteins were found to be overlap and associated with multiple metabolic pathways. Moreover, both the acetylation and succinylation were found in many antimicrobial resistance (AMR) proteins, suggesting its potentially vital role in antibiotic resistance. In general, our work provides insights into the acetylome and succinylome features responsible for the antibiotic resistance mechanism of E. tarda, which may facilitate future investigations on the pathogenesis of this bacterium.