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Parallel reaction monitoring (PRM) analysis was used to confirm changes in abundance of the target proteins (AceF, SodA, YopD, YopE, GroEL, TerE, and OsmY2),. Equal amounts of proteins from the culture supernatants and cell pellets were separated by SDS-PAGE, and bands corresponding to each of the target proteins were subjected to in-gel digestion. The peptide samples for the target proteins were then analyzed by mass spectrometry, and three peptides from each target protein were selected for the PRM analysis. The selection criterion for the peptides was a sequence length of 6–15 amino acids, while peptides with any modifications or missed cleavage sites were excluded. The peak area of three b-/y-ions from each peptide was used to calculate the peptide ratio, and the ratios of three peptides were used to determine the target protein ratio in different samples.