Abstract
Many of the effects of calcium ions in eukaryotic cells are mediated by calcium-binding regulatory proteins such as calmodulin, in which each calcium-binding site has a distinctive helix–loop–helix conformation termed the EF hand1,2. Protein S from the spore coat of the Gram-negative bacterium Myxococcus xanthus has been shown to resemble calmodulin in its internally-duplicated structure and ability to bind calcium3. However, it has a β-sheet secondary structure4,5 rather than the helix–loop–helix arrangement of the eukaryotic proteins. We have determined the complete amino-acid sequence of a calcium-binding protein6 from the Gram-positive bacterium "Streptomyces erythraeus" by cloning and sequencing the corresponding gene. It contains four EF-hand motifs bearing remarkable sequence similarity to the calcium-binding sites in calmodulin. This implies that the EF-hand super-family may have evolved from ancient proteins present in prokaryotes.
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Swan, D., Hale, R., Dhillon, N. et al. A bacterial calcium-binding protein homologous to calmodulin. Nature 329, 84–85 (1987). https://doi.org/10.1038/329084a0
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DOI: https://doi.org/10.1038/329084a0
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