Upload new files. The succinylated modification on bacterial protein lysine residues is currently reported to be crucial for regulating cellular physiology and pathology. In this study, to investigate the effect of the lysine succinylation modification on the biological regulation in a well-known fish pathogen, Aeromonas hydrophila, a highly affinity purification was performed to enrich lysine succinylation peptides in A. hydrophila and then identified a total 2174 lysine succinylation sites on 666 proteins with LC-MS/MS. The further motif analysis showed eight motifs surrounding the central lysine succinylated residue were conservative which share some common preferences with other bacterial species. Gene ontology analysis showed that these succinylated proteins involved in diverse metabolic pathways and biological processes, such as translation, protein export and central metabolic pathways. In general, our study provides a significant insight into the functions of lysine succinylation in the cellular physiology and pathology in A.hydrophila.