PauA: a novel plasminogen activator from Streptococcus uberis

Chromosomal DNA from two geographically distinct isolates of Streptococcus uberis was used to clone the plasminogen activator in an active form in Esc herichia coli. The cloned fragments from each strain contained four potenti al open reading frames (ORFs). That for the plasminogen activator encoded a protein of 286 amino acids (33.4 kDa) which is cleaved between residues 25 and 26 during secretion by S. uberis. The amino acid sequence of the matur e protein showed only weak homology (23.5-28%) to streptokinase. The plasmi nogen activator gene, pauA, in S. uberis was located between two ORFs with high homology to the DNA mismatch repair genes, hexA and hexB, and not on a DNA fragment between the genes encoding an ATP binding cassette transporte r protein (abc) and a protein involved in the formation and degradation of guanosine polyphosphates (rel) as is the case for streptokinase in other st reptococci. (C) 1999 Federation of European Microbiological Societies. Publ ished by Elsevier Science B.V. All rights reserved.