Arthrobacter arilaitensis Re117 protease described here is the first Arthrobacter alkaline metalloprotease studied. It was purified to homogeneity by Sephadex G-100 gel filtration, ultrafiltration, and Mono Q-Sepharose with 3.72-fold increase in specific activity and 28.22% recovery. The molecular mass of the purified enzyme was estimated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) at 50 kDa. The N-terminal amino acid sequence QASTAYSQIDDF, showed high homology with Pseudomonas metalloproteases. The enzyme was highly active over a wide range of pH from 6.0 to 11.0, with an optimum activity at pH 9.0 and $40^{circ}C$. The proteolytic activity was totally lost in the presence of Ethylene Diamine Tetraacetic Acid. Among the tested protein substrates, casein served as the most preferred for the enzyme, followed by fibrin. Purified metalloprotease exhibited significant stability and compatibility with nonionic surfactants (Tween 20, Tween 80, and Triton X-100), oxidizing agents ($H_2O_2$ and sodium perborate), and most of the tested commercial laundry detergents, demonstrating its feasibility for inclusion in detergent formulations.