PMID:2040429
| Citation |
Mottl, H, Terpstra, P and Keck, W (1991) Penicillin-binding protein 4 of Escherichia coli shows a novel type of primary structure among penicillin-interacting proteins. FEMS Microbiol. Lett. 62:213-20 |
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| Abstract |
The nucleotide sequence of a 1884 bp DNA fragment of E. coli, carrying the gene dacB, was determined. The DNA codes for penicillin-binding protein 4 (PBP4), an enzyme of 477 amino acids, being involved as a DD-carboxypeptidase-endopeptidase in murein metabolism. The enzyme is translated with a cleavable signal peptide of 20 amino acids, which was verified by sequencing the amino-terminus of the isolated protein. The characteristic active-site fingerprints SXXK, SXN and KTG of class A beta-lactamases and penicillin-binding proteins were located in the sequence. On the basis of amino acid alignments we propose, that PBP4 and class A beta-lactamases share a common evolutionary origin but PBP4 has acquired an additional domain of 188 amino acids in the region between the SXXK and SXN elements. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/metabolism; Base Sequence; Biological Evolution; Carrier Proteins/chemistry; Carrier Proteins/genetics; Carrier Proteins/metabolism; DNA, Bacterial; Escherichia coli/genetics; Escherichia coli Proteins; Hexosyltransferases; Molecular Sequence Data; Muramoylpentapeptide Carboxypeptidase/chemistry; Muramoylpentapeptide Carboxypeptidase/genetics; Muramoylpentapeptide Carboxypeptidase/metabolism; Nucleotide Mapping; Penicillin-Binding Proteins; Penicillins/metabolism; Peptidyl Transferases; Sequence Alignment; Serine-Type D-Ala-D-Ala Carboxypeptidase; beta-Lactamases/genetics |
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