We have previously reported a powerful promoter from the Streptomyces cinnamoneus TH-2 strain named ‘scmp’ and created an expression vector of pTONA5a based on pIJ702 for expression using S. lividans (Hatanaka et al. (2008) Protein Expr Purif 62: 244-248). The full-length scmp promoter sequence consists of 424 bp upstream of a metalloendoprotease gene in the S. cinnamoneus TH-2 genome. The promoter works in the presence of inorganic phosphate and glucose. In this study, we present the essential region of the scmp promoter (promoter C), which lacks 358 bp of the 5′ region of the full-length promoter. Promoter C was very short and contained only 63 bp. Moreover, there was no restriction on the medium component by combining the promoter and the S. livians 1326 strain. Using promoter C and S. lividans, we succeeded in the extracellular production of the Streptomyces enzymes leucine aminopeptidase, ferulic acid esterase, and transglutaminase, which possessed signal peptides for secretion via the second pathway, at high levels.