Distribution, classification, domain architectures and evolution of prolyl oligopeptidases in prokaryotic lineages.
Distribution, classification, domain architectures and evolution of prolyl oligopeptidases in prokaryotic lineages.
复制标题
原核谱系中丙酰寡肽酶的分布,分类,结构结构和进化。
DOI:
10.1186/1471-2164-15-985
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发表时间:
2014-11-18
期刊:
影响因子:
4.4
通讯作者:
Sowdhamini R
中科院分区:
文献类型:
--
作者:
Kaushik S;Sowdhamini R
Prolyl oligopeptidases (POPs) are proteolytic enzymes, widely distributed in all the kingdoms of life. Bacterial POPs are pharmaceutically important enzymes, yet their functional and evolutionary details are not fully explored. Therefore, current analysis is aimed at understanding the distribution, domain architecture, probable biological functions and gene family expansion of POPs in bacterial and archaeal lineages. Exhaustive sequence analysis of 1,202 bacterial and 91 archaeal genomes revealed ~3,000 POP homologs, with only 638 annotated POPs. We observed wide distribution of POPs in all the analysed bacterial lineages. Phylogenetic analysis and co-clustering of POPs of different phyla suggested their common functions in all the prokaryotic species. Further, on the basis of unique sequence motifs we could classify bacterial POPs into eight subtypes. Analysis of coexisting domains in POPs highlighted their involvement in protein-protein interactions and cellular signaling. We proposed significant extension of this gene family by characterizing 39 new POPs and 158 new α/β hydrolase members. Our study reflects diversity and functional importance of POPs in bacterial species. Many genomes with multiple POPs were identified with high sequence variations and different cellular localizations. Such anomalous distribution of POP genes in different bacterial genomes shows differential expansion of POP gene family primarily by multiple horizontal gene transfer events. The online version of this article (doi:10.1186/1471-2164-15-985) contains supplementary material, which is available to authorized users.