Department of Microbiology, Kazan (Volga region) Federal University, Kazan, Russia.
FEBS Lett. 2010 Nov 5;584(21):4419-25. doi: 10.1016/j.febslet.2010.09.049. Epub 2010 Oct 8.
The mprBi gene from Bacillus intermedius 3-19 encoding a novel secreted metalloproteinase was identified. The mpriBi gene was expressed in an extracellular proteinase-deficient Bacillus subtilis BG 2036 strain and the corresponding protein was characterized biochemically. The 19 kDa MprBi protein was purified to homogeneity and sequenced by mass spectroscopy and Edman degradation methods. Amino acid sequence analysis of MprBi identified an active site motif HEYGHNFGLPHD and a conserved structural component Met-turn, both of which are unique features of the metzincin clan. Furthermore, MprBi harbors a number of distinct sequence elements characteristic of proteinase domains in eukaryotic adamalysins. We conclude that MprBi and similar proteins from other Bacillus species form a novel group of metzincin metalloproteinases in prokaryotes.
从中间芽孢杆菌 3-19 中鉴定出编码新型分泌金属蛋白酶的 mprBi 基因。mprBi 基因在胞外蛋白酶缺陷型枯草芽孢杆菌 BG2036 菌株中表达,并对相应的蛋白进行了生化特性分析。19 kDa 的 MprBi 蛋白经纯化达到均一性,并通过质谱和 Edman 降解方法进行测序。MprBi 的氨基酸序列分析鉴定出一个活性位点基序 HEYGHNFGLPHD 和一个保守的结构成分 Met-turn,这两者都是 metzincin 家族的独特特征。此外,MprBi 还具有许多独特的序列元件,这些元件是真核 adamalysin 蛋白酶结构域的特征。我们得出结论,MprBi 和来自其他芽孢杆菌属的类似蛋白在原核生物中形成了一类新型的 metzincin 金属蛋白酶。