Abstract:Xanthomonas campestris belong to Gram-negative bacteria, which mainly harm cruciferous vegetables and economic forests such as walnuts and mangosteens, causing great economic losses to agricultural and forestry crops and seriously harming the healthy development of the agricultural and forestry industry. Secreted proteins play an important role in the pathogenic process of plant pathogenic fungi, bacteria, and oomycetes. There have been no reports on the physical and chemical properties and characteristics of secreted proteins of Xanthomonas. This study uses the secreted protein sequences of X. campestris B100, X. campestris pv. campestris str.8004, and X. campestris CN14 with the published genome-wide sequence as the basic data, and uses Protscale, SMART, TargetP 2.0 Server, and other organisms. Informatics analysis software analyzes the physicochemical properties, conserved domains, and transit peptides of the above-secreted proteins. The results show that there are no obvious rule between the theoretical isoelectric point of secreted proteins in X. campestris and the length of amino acids. The average 44.73% of the protein is Unstable protein, with an average of 83.21% of the total protein, the average hydrophilicity is less than 0, which is a hydrophilic protein. At the same time, 12 of the secreted proteins of each X. campestris have an obvious conserved domain, and all secreted The protein is localized at S (signal peptide), and the predicted probability distribution of the transit peptide is also relatively even. This study lays a solid theoretical foundation for the in-depth analysis of the function of X. campestris secreted proteins.