Phylogeny of phosphoryl transfer proteins of the phosphoenolpyruvate-dependent sugar-transporting phosphotransferase system
Phylogeny of phosphoryl transfer proteins of the phosphoenolpyruvate-dependent sugar-transporting phosphotransferase system
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DOI：
10.1016/s0923-2508(02)01339-6
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发表时间：
2002-09-01
影响因子：
2.6
通讯作者：
Saier, MH
中科院分区：
文献类型：
--
作者：
Hu, KY;Saier, MH
一些细菌缺乏细菌磷酸转移酶系统（PTS）的糖渗透酶，但在它们的基因组中编码可能在调节中起作用的PTS的磷酰基转移蛋白。这些蛋白质包括HPr（PtsH）、ATP依赖性HPr（ser）激酶/磷酸酶（PtsK）和PEP依赖性HPr（his）激酶（称为酶I（PtsI））的同源物。我们确定了所有目前测序的这些蛋白质的同源物，多重比对它们的序列，并构建系统发育树，以获得功能，结构和进化的结论。我们发现，没有细菌拥有一个以上的HPr激酶，这些蛋白质可能都是orthopolysaccharide。α-变形菌具有截短的HPr激酶，其可能与其他PTS蛋白一起发挥统一的调节功能。酶I在所有革兰氏阳性菌和一些革兰氏阴性菌中是直链的，但其他革兰氏阴性菌显示出5种功能类型的旁系同源物。没有一种具有完全测序基因组的细菌表现出所有这些类型。除了经典的酶1之外，这些功能类型中的每一种都表现出一组独特的伴随结构域，通常具有特征性的结构域顺序。一种功能类型，即果糖特异性类型，包括具有不同结构域顺序的两个遗传学上不同的亚组。结果表明，域协会发生在PTS的进化历史的早期，随后的域重排很少发生。我们的研究结果定义了这些重要的细菌蛋白质的进化历史，并为基因组测序揭示的基因编码的PTS相关蛋白质的功能分配提供指导。(C)2002年，Elsevier SAS科学与医学版。All rights reserved.
Some bacteria lack sugar permeases of the bacterial phosphotransferase system (PTS) but encode within their genomes phosphoryl transfer proteins of the PTS that probably function in regulation. These proteins include homologues of HPr (PtsH), the ATP-dependent HPr(ser) kinase/phosphatase (PtsK) and the PEP-dependent HPr(his) kinase known as Enzyme I (PtsI). We identify all currently sequenced homologues of these proteins, multiply align their sequences and construct phylogenetic trees in order to derive functional, structural and evolutionary conclusions. We show that no bacterium possesses more than one HPr kinase and that these proteins are probably all orthologous. alpha-Proteobacteria possess truncated HPr kinases which probably serve a unified regulatory function together with other PTS proteins. The Enzymes I are orthologous in all Gram-positive bacteria and some Gram-negative bacteria, but other Gram-negative bacteria exhibit paralogues that fall into 5 functional types. No bacterium with a fully sequenced genome exhibits all of these types. With the exception of the classical Enzymes 1, each of these functional types exhibits a distinctive set of accompanying domains, usually with a characteristic domain order. One functional type, the fructose-specific type, includes two phylogenetically different subgroups with different domain orders. The results establish that domain associations occurred early during evolutionary history of the PTS, and that subsequent domain rearrangements occurred rarely. Our findings define the evolutionary histories of these important bacterial proteins and provide guides for functional assignment of PTS-related proteins encoded by genes revealed by genome sequencing. (C) 2002 Editions scientifiques et medicales Elsevier SAS. All rights reserved.