Comamonas testosteroni antA encodes an antimonite-translocating P-type ATPase.

ABSTRACT: Antimony, like arsenic, is a toxic metalloid widely distributed in the environment. Microbial detoxification of antimony has recently been identified. Here we describe a novel bacterial P_1B-type antimonite (Sb(III))-translocating ATPase from the antimony-mining bacterium Comamonas testosterone JL40 that confers resistance to Sb(III). In a comparative proteomics analysis of strain JL40, an operon (ant operon) was up-regulated by Sb(III). The ant operon includes three genes, antR, antC and antA. AntR belongs to the ArsR/SmtB family of metalloregulatory proteins that regulates expression of the ant operon. AntA belongs to the P_1B family of the P-type cation-translocating ATPases. It has both similarities to and differences from other members of the P_1B-1 subfa

SUBMITTER: An L 

PROVIDER: S-EPMC7885177 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature