Abstract
CLC chloride-transport proteins are expressed ubiquitously and are vital to several physiological processes. This family is distinctive in that some members are chloride ion channels while others are chloride/proton antiporters. To better understand the mechanistic similarities and differences between CLC proteins, we have characterized a novel bacterial homolog from Citrobacter koseri called CLC-b. CLC-b is 24% identical and 42% similar in amino acid sequence to CLC-ec1, but lacks several amino acids near the chloride binding sites that are conserved in most CLCs.
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