LPS-Dephosphorylating Alkaline Phosphatase of PhoA Family Divergent from the Multiple Homologues of spp.

A highly active alkaline phosphatase (ALP) of the protein structural family PhoA, from a mussel gut-associated strain of the marine bacterium KMM 296 (CmAP), was found to effectively dephosphorylate lipopolysaccharides (LPS). Therefore, the aim of this work was to perform a comprehensive bioinformatics analysis of the structure, and to suggest the physiological role of this enzyme in marine bacteria of the genus . A scrutiny of the CmAP-like sequences in 36 available genomes revealed nine homologues intrinsic to the subspecies , whereas PhoA of a distant relative JO1 carried an inactive mutation.