An extracellular phospholipase D ($PLD_{St}$) was purified from Streptomyces tendae by two successive chromatographic steps on Sepharose CL-6B and DEAE-Sepharose CL-6B. Molecular weight of the $PLD_{St}$ was estimated to be approximately 43 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Maximal activity was at pH 8 and $60^{circ}C$, and the enzyme was stable at or below $60^{circ}C$ and between pH 8 and 10, when assayed after 1.5 and 24 h, respectively. The enzyme activity had an absolute requirement of $Ca^{2+}$, and the maximum activity was at 2 mM $CaCl_2$. The Km and Vmax values for phosphatidyl choline were 0.95 mM and $810;{mu}mol;min^{-1}mg^{-1}$, respectively. More importantly, PLDSt could not catalyze transphosphatidylation of glycerol, L-serine, myo-inositol and ethanolamine, which have been extensively used to evaluate the activity. The result strongly suggests that $PLD_{St}$ does not have the transphosphatidylation activity, thereby making it the first Streptomyces PLD possessing only hydrolytic activity. $PLD_{St}$ may therefore be a novel type of PLD enzyme.