A thermophilic laccase has been identified in an extremely thermophilic bacterium when grown in the presence of copper. The protein was purified and the gene was cloned, sequenced, and expressed in Escherichia coli. The recombinant enzyme displayed a blue color typical of laccases and copper-dependent oxidase activity on canonical laccase substrates such as guaiacol, 2, 6-dimethoxyphenol, 2, 2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate), and syringaldazine at acidic pH. The enzyme was most notable for its striking thermophilicity; the optimal reaction temperature was ~92°C and a half-life of thermal inactivation at 80°C was >14 h, ranking it the most thermophilic laccase reported thus far.