Isolation and characterization of a moderately halophilic bacterium, Virgibacillus sp. EMB13, from the West coast of India has been described in the present study. It produced five different extracellular proteases. Conditions were optimized for maximum protease production. Under optimized conditions, viz., a medium containing (%, w/v) yeast extract, 1.0; peptone, 0.5; mannitol, 0.5; NaCl, 0.5; KCl, 1.0; CaCl2, 0.03 and MgSO4, 0.04 with pH 8, it produced 270 U protease mL(-1). The protease was partially purified by DEAE ion exchange and Sephadex G-75 gel filtration chromatography. The purified preparation contained two unseparated proteases with apparent molecular masses of 49 and 54 kDa, respectively. The preparation was stable at different concentrations of NaCl (0-15%, w/v) and pH range 6.0-12.0. It exhibited maximal activity at pH 7.5, temperature 50 degrees C and 1% (w/v) NaCl. The K-m and V-max, values towards casein were 7.5 mg mL(-1) and 156.25 mu g min(-1) mL(-1), respectively. Inhibition of their proteolytic activity by EDTA and 1,10-phenanthroline indicated them to be metalloprotease in nature. The proteases exhibited remarkable stability in the presence of salt and organic solvents. These properties enable them for novel applications in non-aqueous enzymology and as an additive in detergent formulations.