Abstract: [Objective] To predict and analyze the structure and function of Cronobacter malonaticus protein OmpA. [Methods] The amino acid sequence of protein OmpA of Cronobacter malonaticus was obtained from the NCBI database. The physicochemical and hydrophilic properties of the protein OmpA were analysed by using ProtParam tool and ProtScal tool. SignalP 5.0 tool TMHMM 2.0 tool and NetPhos 3.1 were used to analyze the signal peptides, transmembrane regions, and phosphorylation sites of protein OmpA. The secondary structure of protein OmpA was predicted by using modified SOPMA algorithm. The tertiary structure of protein OmpA was predicted by using SWISS-MODEL tool. Meanwhile, B cell epitopes and T cell epitopes of protein OmpA were predicted by using BepiPred tool and SYFPEITHI tool. Interaction proteins of protein OmpA were analyzed by using STRING tool. [Results] The protein OmpA of Cronobacter malonaticus LMG 23826 contains 347 amino acids. The protein has the following characteristics: Its property is a stable hydrophobic protein. The protein has signal peptides but no transmembrane regions, indicating that it was located outside the membrane of bacteria. [Conclusion] The OmpA protein is hydrophobic puter membrane protein with potential B and T cell epitopes. These findings provide a theoretical reference for study of the antigenicity of Cronobacter malonaticus and for development of highly efficient epitopebased vaccines.

Key words: OmpA protein, structure, function, feature algorithm program, bioinformatics