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We have designed a fusion protein consisting of a domain that binds strongly to zinc, cobalt and cadmium and the C-terminus of the Pseudomonas sp. lipase (PML), which acts as a secretion tag for E. coli cells containing the lipBCD genes from S. marcescens. We would like our system to be as sustainable and low-cost as possible so that it, or an improved version of it, would be practical and applicable in developing nations where contaminated water supplies are especially problematic. We hope that using a protein secretion system will help us achieve that goal by providing us with an easy, low energy means to purify the metal filtering fusion protein. In this scheme, the same population of E. coli can be used to produce our protein multiple times since the protein would accumulate in the growth media and not within the cells, in which case we would need to lyse the E. coli in order to prepare each filter.