Nucleotide sequencing of a polyurethanase gene (pulA) from Pseudomonas fluorescens

Nucleotide sequencing of a gene (pulA) encoding an extracellular polyurethanase/esterase from Pseudomonas fluorescens revealed an open reading frame encoding a 48 kDa protein of 451 amino acid residues. The deduced polypeptide sequence contained a serine-hydrolase consensus sequence GXSXG. The polypeptide lacked an N-terminal signal peptide, but did contain a short region toward the C-terminus that has been observed in secreted lipases, EXXXGXTFIIGSXGNDXIXGGXGXDXXEXXXGXD. The most closely related proteins to the polyurethanase had amino acid sequence homologies of 71%, 67%, 69%, 67% for lipases from P. fluorescens, and 51% for lipases from Serratia marcescens.