Reizer J, Reizer A, Perego M, Saier M H
Department of Biology, University of California at San Diego, La Jolla, USA.
Microb Comp Genomics. 1997;2(2):103-11. doi: 10.1089/omi.1.1997.2.103.
We have characterized a novel family of response regulator aspartyl-phosphate (RAP) phosphatases found exclusively in gram-positive bacteria. The family consists of 15 members, 12 of which are from Bacillus subtilis. The N-terminal domains proved to be more highly conserved than the C-terminal domains, and a signature sequence for the family was derived from the former domains. Phylogenetic analyses revealed clustering patterns showing that all Bacillus proteins are closely related. Most of the Bacillus RAP phosphatase genes are followed by and are translationally coupled to small nonhomologous phosphatase regulator (phr) genes that encode exported peptides with regulatory functions. Most of the paralogous RAP phosphatases of B. subtilis may serve related functions in signal transduction systems. They appear to have arisen by relatively recent gene duplication events that occurred after the divergence of major groups within the gram-positive bacterial kingdom. We suggest that the N-terminal domains of the RAP phosphatases function in catalysis, whereas the C-terminal domains function in regulation.
我们鉴定了一个仅在革兰氏阳性菌中发现的新型应答调节天冬氨酰磷酸（RAP）磷酸酶家族。该家族由15个成员组成，其中12个来自枯草芽孢杆菌。结果表明，N端结构域比C端结构域保守性更高，并且该家族的一个特征序列源自前者。系统发育分析揭示的聚类模式表明，所有芽孢杆菌属蛋白都密切相关。大多数枯草芽孢杆菌RAP磷酸酶基因后面都有小的非同源磷酸酶调节（phr）基因，并且它们在翻译上偶联，这些phr基因编码具有调节功能的输出肽。枯草芽孢杆菌的大多数旁系同源RAP磷酸酶可能在信号转导系统中发挥相关功能。它们似乎是在革兰氏阳性细菌界主要类群分化之后通过相对较新的基因复制事件产生的。我们认为，RAP磷酸酶的N端结构域在催化中起作用，而C端结构域在调节中起作用。
