SUMMARY: The gene coding for coagulase () was cloned from 8325-4 in a λ replacement vector in Coagulase (plasma-clotting) activity was measured in λ lysates and an immunoreactive protein of 60 kDa was detected by Western immunoblotting with anti-coagulase serum. This protein comigrated with the major immunoreactive protein in supernatants of 8325-4. The gene was subcloned in pUC vectors. One recombinant expressed a 60 kDa immunoreactive protein and plasma-clotting activity. A putative β-galactosidase-coagulase fusion protein and truncated peptides were expressed by variants formed by subcloning. These results are consistent with previously published biochemical data that the prothrombin-binding domain of coagulase is located in the N-terminus of the protein. The cloned gene was transferred into on a shuttle plasmid. Expression of coagulase was higher in a strain with a mutation in the locus, which controls the level of several exoproteins in , suggesting that normally regulates coagulase expression negatively.


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