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. 1992 Feb 1;111(1):125-30.
doi: 10.1016/0378-1119(92)90613-t.

Cloning and characterization of a gene encoding extracellular metalloprotease from Streptomyces lividans

H S Lichenstein  1 , L A Busse, G A Smith, L O Narhi, M O McGinley, M F Rohde, J L Katzowitz, M M Zukowski
Affiliations

Cloning and characterization of a gene encoding extracellular metalloprotease from Streptomyces lividans

H S Lichenstein et al. Gene. .

Abstract

The prt gene, encoding a protease (Prt) from Streptomyces lividans TK24, was cloned and sequenced. An S. lividans host with plasmid-borne prt secreted 200 micrograms/ml of a 22-kDa Prt into the culture medium. Prt is classified as a metalloprotease since its activity is significantly inhibited by 1,10-phenanthroline or EDTA. The region upstream from prt codes for an incomplete open reading frame (ORF) oriented opposite to prt. This ORF has a strong similarity to a gene family (lysR) whose members regulate the transcription of structural genes required for either biosynthesis or degradation.

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