Distribution, classification, domain architectures and evolution of prolyl oligopeptidases in prokaryotic lineages.

ABSTRACT:

Background

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.

Results

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. Fur

SUBMITTER: Kaushik S 

PROVIDER: S-EPMC4522959 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature