Nucleotide sequence of the gene for the peptidoglycan-associated lipoprotein of Escherichia coli K12.

During attempts to clone the gene for the Escherichia coli outer membrane protein III another gene was recovered. Its nucleotide sequence was determined and the deduced amino acid sequence showed that the gene does not encode protein III. It codes for a 173-residue polypeptide; 21 NH2-terminal residues are typical for a signal peptide. The sequence around the putative site (Ala-Cys) for removing this peptide, Ala-Ile-Ala-Ala-Cys-Ser-Ser-Asn, is highly homologous to that of the major cell envelope lipoprotein (Braun lipoprotein) surrounding its processing site; it is also homologous to the consensus pentapeptide Leu-Leu-Ala-Gly-Cys present in other lipoproteins of gram-negative bacteria. It could be shown that the gene expresses a lipoprotein with all the properties, including the amino acid composition, of the peptidoglycan-associated lipoprotein (PAL) [Mizuno, T. (1979) J. Biochem. (Tokyo) 86, 991-1000]. Therefore, the cloned gene is the pal gene. The protein does not contain hydrophobic regions which would serve as a membrane anchor. Tandemly repeated amino acid sequences exist at and near the NH2-terminus of the mature protein which are homologous to such repeats in the Braun lipoprotein, suggesting a common origin of this part of the two proteins. Attempts to place a transposon into the pal gene were unsuccessful. Hence the complete absence of the protein may be lethal and its function remains unknown.