The proline iminopeptidase (PepIP) of subsp. is a major peptidase located in the cell envelope. Its structural gene () has been cloned into pUC18 and expressed at a very high level in to give a IP activity 15000-fold higher than that found in subsp. . The nucleotide sequence of the gene revealed an open reading frame of 295 codons encoding a protein with a predicted of 33006, which is consistent with the apparent size of the gene product. The amino acid sequence of PepIP shows significant homology with those of other hydrolases involved in the degradation of cyclic compounds. In particular, there is a region which includes an identified catalytic site containing a serine residue and a motif specific for the active sites of prolyloligopeptidases (Gly-X-Ser-X-Gly-Gly). The PepIP opens a new way for supplying cells with proline using the peptides resulting from the proteolytic degradation of caseins.


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