PilZ domain is part of the bacterial c-di-GMP binding protein
PilZ domain is part of the bacterial c-di-GMP binding protein
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DOI：
10.1093/bioinformatics/bti739
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发表时间：
2006-01-01
期刊：
影响因子：
5.8
通讯作者：
Galperin, MY
中科院分区：
文献类型：
--
作者：
Amikam, D;Galperin, MY
最近的研究发现，c-di-GMP是一种普遍存在的细菌次级信使，调节各种细菌的生物膜形成、运动、胞外多糖的产生和多细胞行为。然而，除了纤维素合成酶以外，还没有发现与c-di-GMP结合的蛋白质，c-di-GMP的作用靶点也尚不清楚。在这里，我们报告了在细菌纤维素合成酶、藻酸盐生物合成蛋白AL44、肠杆菌YcgR和FirmicutYpfA家族的蛋白以及其他在细菌基因组中编码的蛋白的序列中发现了Pilz结构域(PF07238)，并有证据表明该结构域是长期寻找的c-di-GMP结合蛋白的一部分。Pilz结构域与许多其他结构域的结合，包括细菌多药分泌系统的可能成分，可能为c-di-GMP在细菌发病机制和细胞发育中的多种功能提供线索。
Recent studies identified c-di-GMP as a universal bacterial secondary messenger regulating biofilm formation, motility, production of extracellular polysaccharide and multicellular behavior in diverse bacteria. However, except for cellulose synthase, no protein has been shown to bind c-di-GMP and the targets for c-di-GMP action remain unknown. Here we report identification of the PilZ ('pills') domain (Pfam domain PF07238) in the sequences of bacterial cellulose synthases, alginate biosynthesis protein Alg44, proteins of enterobacterial YcgR and firmicute YpfA families, and other proteins encoded in bacterial genomes and present evidence indicating that this domain is ( part of) the long-sought c-di-GMP-binding protein. Association of the PilZ domain with a variety of other domains, including likely components of bacterial multidrug secretion system, could provide clues to multiple functions of the c-di-GMP in bacterial pathogenesis and cell development.