[Objective] This study aimed to get more information about sequence and protein structure of type IV lanthipeptide synthetases. [Methods] Eight potential type IV lanthipeptide synthetases were chosen from Bacillus subtilis, Streptomyces collinus Tu 365, Lactobacillus iners LactinV, Streptococcus pneumoniae, Lactobacillus delbruecki, Bifidobacterium longum, Amycolatopsis azurea and Finegoldia magna, and their physicochemical properties, domains, secondary structures were analyzed and predicted using different softwares. By using the Neighbor-joining method of Molecular Evolutionary Genetics Analysis software, a dendrogram was obtained based on genetic distances. [Results] All eight proteins were hydrophilicity and there was no signal peptide in them. The proteins in S. collinus Tu 365, B. subtilis, S. pneumoniae, Lactobacillus delbruecki, Bifidobacterium longum, Amycolatopsis azurea and Finegoldia magna were acidic whereas the others were alkaline. The proteins in S. collinus Tu 365, B. subtilis and S. pneumoniae were unstable whereas the others were stable. The evolutionary analysis showed that B. subtilis had the closest genetic relationship with S. pneumonia. The evolutionary relationships of LANC-like domains were similar to total synthase, which was different from STYKc/S_TKc domains. Alpha helix and coil were the basic secondary structure. All those proteins contained LANC-like domain. [Conclusion] All that eight synthetases have their conservative structure in different bacteria, therefore, they can play the similar biological functions. All these results will provide information of the type IV lanthipeptide synthetase for further study, especially for improving the bio-control value of B. subtilis.