The genome of Deinococcus sp. RM strain and its transcriptome in the process of chicken feather degradation were sequenced, the protease gene with high expression was selected and recombined in Pichia pastoris GS115 strain for induction expression. The purification, enzymatic properties and the effects of chicken feather degradation of the recombinant protease were determined. The results showed that RM strain had 4 132 genes and 3 844 genes expressed, of which 444 genes expressed extracellular proteins and 26 were extracellular proteases. The high expression gene sp02200 was successfully expressed in the P. pastoris GS115 strain. The recombinant protease rSp02200 belonged to a novel DegQ protease of high-temperature requirement family, with an optimal reaction temperature of 37 ℃, and remained good stability below 30 ℃. The optimal pH was 7.5, and maintained more than 70% protease activity at pH 4.0-11.0. The protease can degrade long and thick feather axes and branches into small feather axes and branches. Therefore, Sp02200 protease was an important protease in the chicken feather degradation process of RM strain, which provides a reference for exploring related genes involved in feather degradation of RM strain.