Protease secretion by Erwinia chrysanthemi. Proteases B and C are synthesized and secreted as zymogens without a signal peptide.

The gene encoding the secreted 53-kDa metalloprotease (protease B) and the 5' end of the gene encoding the secreted 55-kDa metalloprotease (protease C) of the Gram-negative bacterium Erwinia chrysanthemi have been sequenced. The predicted sequences of the two proteases do not have typical signal sequences at their NH2 termini. Both proteases are synthesized as inactive higher molecular weight precursors (zymogens proB and proC) which are secreted into the external medium where divalent cation-mediated activation occurs. The activation of proB occurs with a t1/2 of less than 5 min at 37 degrees C in Luria broth medium, whereas that of proC occurs with a t1/2 of about 150 min. The NH2 termini of purified proteases B, proB, and C were sequenced. ProB starts at the initiator methionine whereas B and C start, respectively, at residues +16 and +18 of the sequence deduced from the nucleotide sequence. A short NH2-terminal extension is therefore removed during the activation process, most likely by an autocatalytic mechanism. Protease B shows a high degree of sequence homology with the secreted 50-kDa metalloprotease of Serratia marcescens, which also lacks a signal peptide and for which an inactive higher molecular weight form has been reported.