ArticleBMC genomics2014
Distribution, classification, domain architectures and evolution of prolyl oligopeptidases in prokaryotic lineages.
Article in BMC genomics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP.Nature communications · 2025Article
- Comparative analysis of thermal adaptations of extremophilic prolyl oligopeptidases.Biophysical journal · 2024Article
- Reducing Immunoreactivity of Gluten Peptides by Probiotic Lactic Acid Bacteria for Dietary Management of Gluten-Related Diseases.Nutrients · 2024Article
- Early transcriptional changes of heavy metal resistance and multiple efflux genes in Xanthomonas campestris pv. campestris under copper and heavy metal ion stress.BMC microbiology · 2024Article
- Gluten-degrading bacteria: availability and applications.Applied microbiology and biotechnology · 2021Review
- Altitudinal variation of the gut microbiota in wild house mice.Molecular ecology · 2019Article
- Crystal Structure and Conformational Dynamics of Pyrococcus furiosus Prolyl Oligopeptidase.Biochemistry · 2019Article
- The MSDIN family in amanitin-producing mushrooms and evolution of the prolyl oligopeptidase genes.IMA fungus · 2018Article
- Biosynthetic Proteases That Catalyze the Macrocyclization of Ribosomally Synthesized Linear Peptides.Biochemistry · 2018Review
- Functional metagenomics of oil-impacted mangrove sediments reveals high abundance of hydrolases of biotechnological interest.World journal of microbiology & biotechnology · 2017Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundProlyl 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.
resultsExhaustive 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.
conclusionsOur 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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.