Bioinformatics Analysis of the Structure and Function of EdeB from Brevibacillus brevis X23

Brevibacillus Brevis X23 is widely used in the biological control of plant diseases. It can produce antibacterially active substances—edeines. EdeB protein is a potential regulator of edeines biosynthesis. Analyzing its bioinformatics information may lay a foundation for the further study of the function of EdeB protein in the process of antibiotic biosynthesis. Based on the amino acid sequence of EdeB protein from NCBI database, the bioinformatics analyses were performed to analyze its protein physical and chemical properties, transmembrane region, signal peptide, tertiary structure, phosphorylation sites and glycosylation sites. The results showed that EdeB protein was composed of 256 amino acids. It had a relative molecular weight of 30.42 kDa and a theoretical isoelectric point (pI) of 6.23. It was a hydrophilic protein without signal peptide or transmembrane. Its secondary structure mainly consisted of α-helices and random coil. The tertiary structural model for EdeB protein was successfully built. The EdeB protein belonged to the ParB family, suggesting its biological function of regulation by DNA-binding. It was predicted to have 16 phosphorylation sites, 1 N-glycosylation site and 20 O-glycosylation sites. This study can provide a theoretical basis for the function and mechanism of action of EdeB protein.