Abstract
Gram positive bacteria possess metal dependent regulator proteins (MdeRs) which regulate the uptake and efflux of metal ions. MdeRs share a common fold yet are highly diverse in sequence space, often sharing less than 20% sequence identity. Further, MdeRs exhibit important differences in metal binding and specificity. In this study, we determined the sequence and structural motifs responsible for these differences. We used sequence analysis tools to construct networks of MdeR sequences, then based on network analysis, we identified characteristic sequence and structural metal-binding motifs within each subfamily. Each of these subfamilies possess overlapping, yet unique sequence and structural motifs that may enable different metal ion specificities and modes of activation. This work enhances our current understanding of MdeR function and improves the assignment of specific function within the MdeR family.
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