采用生物信息学分析方法，对沼泽红假单胞菌N-酰基高丝氨酸内酯酶理化性质和结构特征进行预测。结果表明，该蛋白为稳定的亲水性蛋白，定位在细菌的细胞质中，无信号肽结构。二级结构中含有α-螺旋、β-转角、延伸链和无规则卷曲等结构元件，α-螺旋和无规则卷曲对三级结构的稳定和功能发挥具有重要意义。含有6个磷酸化位点，无跨膜结构域。参与细菌群体感应淬灭。

The aim of the present study was to understand the physical and chemical properties and structural characteristic of N-acyl homoserine lactonase in Rhodopseudomonas palustris by bioinformatics method. The results showed that the protein was a stable hydrophilic protein. The protein was localized in the cytoplasm of bacteria. The protein had no signal peptide structure. The secondary structure of the protein contained α-helix， β-angle， extended chain and random coil. The α-helix and random coil played an important role in the stability and function of tertiary structure. The protein contained six phosphorylation sites. The protein had no transmembrane domain. The protein was involved in quorum sensing quenching.

Q939.96

国家自然科学基金(31460595)；江西省教育厅科学技术研究项目(GJJ181090)；南昌师范学院博士科研启动基金(NSBSJJ2018023)；南昌师范学院校级科研项目(20RWYB02)；南昌师范学院“11531”工程。