Diversity and Phylogenetic Distribution of Extracellular Microbial Peptidases.

Depolymerization of proteinaceous compounds by extracellular proteolytic enzymes is a bottleneck in the nitrogen cycle, limiting the rate of the nitrogen turnover in soils. Protein degradation is accomplished by a diverse range of extracellular (secreted) peptidases. Our objective was to better understand the evolution of these enzymes and how their functional diversity corresponds to known phylogenetic diversity. Peptidase subfamilies from 110 archaeal, 1,860 bacterial, and 97 fungal genomes were extracted from the MEROPS database along with corresponding SSU sequences for each genome from the SILVA database, resulting in 43,177 secreted peptidases belonging to 34 microbial phyla and 149 peptidase subfamilies. We compared the distribution of each peptidase subfamily across all taxa to the phylogenetic relationships of these organisms based on their SSU gene sequences. The occurrence and abundance of genes coding for secreted peptidases varied across microbial taxa, distinguishing the peptidase complement of the three microbial kingdoms. The distribution of secreted peptidases was found to be significantly correlated with phylogenetic relationships within kingdoms (archaea r_Mantel=0.364, p=0.001; bacteria r_Mantel=0.257, p=0.001, and fungi r_Mantel=0.281, p=0.005), inferring an evolutionary relationship where subsets of phylogenetically related organisms share similar types of secreted peptidases. About one-third of the peptidase subfamilies displayed a strong evolutionary signal; the rest were phylogenetically over-dispersed, suggesting that these subfamilies are randomly distributed across the tree of life or the result of events such as horizontal gene transfer. Study of the diversity and phylogenetic distribution of secreted peptidases offered a mechanistic basis to anticipate the proteolytic potential function of microbial communities.