An LPS-dephosphorylating alkaline phosphatase of PhoA family from the marine bacteriumCobetia amphilectiKMM 296 and multiplicity of alkaline phosphatase families inCobetiaspp

Abstract

A highly active alkaline phosphatase (ALP) from the mollusk strain of the marine bacteriumCobetia amphilectiKMM 296 (CmAP) was found to remove phosphorus from theEscherichia colilipopolysaccharides (LPS). Phylogenetic analysis of the amino acid sequences of ALPs found in 36 availableCobetiagenomes revealed that CmAP and its homologues from nine strains clustered together with the human and squid LPS-detoxifying enzymes. Each strain of the genusCobetiahas a variety of ALPs mostly of the PhoD and PhoX families. The PhoA gene encoding for the CmAP-like ALP is characteristic for the subspeciesC. amphilecti, with a complete set of four ALP families, including PafA and two PhoD structures (5 genes). However, a single strain of the speciesCobetia crustatorumJO1Tfrom fermented shrimp, phylogenetically distant fromC. amphilectiandC. marina, among four ALPs contains a CmAP homologue carrying an inactive mutation. Apparently, the multiplicity of ALPs in bacteria of the genusCobetiais a trait of incredible adaptation to a phosphorus-depleted environment and a specialty of organophosphate destructor in eco-niches to which they once emerged, includingZosteraspp. roots. The ALP clusterization and an identity level of the genus-specific biosynthetic genes encoding for ectoine and polyketide cluster T1PKS, responsible for sulfated extracellular polysaccharide synthesis, coincide with a new whole genome-based taxonomic classification of the genusCobetia. The LPS-dephosphorylating property of the PhoA familyC. amphilectiALP CmAP may be used in the development of anti-inflammatory drugs.