Bacterial calpains and the evolution of the calpain (C2) family of peptidases. Issue 1 (December 2015)

• Record Type: Journal Article
• Authors: Rawlings, Neil
• Is Part Of: Biology direct. Volume 10:Issue 1(2015)
• Page Start: 1
• Page End: 12
• Publication Date: 2015-12
• Subjects: Calpain -- Calpamodulin -- Androglobin -- Peptidase -- Evolution -- Alignment -- Phylogenetic tree -- Bacteria; Biology -- Periodicals; 570.5
• DOI: 10.1186/s13062-015-0095-0
• Languages: English
• ISSNs: 1745-6150

Abstract

Abstract Homologues of calpain, often thought to be an essential, cytoplasmic, calcium-dependent cysteine endopeptidase found exclusively in eukaryotes, have been found in bacterial proteomes. The homologues lack calcium-binding sites, have differing domain architectures, and can be secreted or membrane-associated. Homologues are rare and occur in a minority of bacterial phyla and often in a minority of species in a genus. However, the differences in domain architecture argue against a recent, horizontal gene transfer from a eukaryote. From analysis of a phylogenetic tree and absence of homologues in archaea, calpains in eukaryotes may be derived from genes horizontally transferred from a bacterium. Reviewers: This article was reviewed by L. Aravind and Frank Eisenhaber.