In this study, we employed multidimensional omics approaches, including proteomics, acetyl-omics, succinyl-omics, and lactyl-omics, to systematically investigate the effects of glucose treatment on protein expression and post-translational modifications in MRSA. Through the application of mass spectrometry, we identified 2,479 lysine acetylation sites, 1,353 lysine succinylation sites, and 89 lysine lactylation sites. Subsequent bioinformatics analyses indicated a significant enrichment of lysine acylations in ribosome-related functions and metabolism-associated pathways. Different types of lysine acylation exhibited distinct regulatory patterns. Further analysis demonstrated that lysine succinylation modulates the enzymatic activity of arsenate reductase, implicating its role in bacterial metabolic adaptation and functional regulation.