Penicillin-binding protein 4 of Escherichia coli shows a novel type of primary structure among penicillin-interacting proteins.
FEMS Microbiol Lett
; 62(2-3): 213-20, 1991 Mar 01.
Article
in En
| MEDLINE
| ID: mdl-2040429
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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Database:
MEDLINE
Main subject:
Penicillins
/
Bacterial Proteins
/
Muramoylpentapeptide Carboxypeptidase
/
Carrier Proteins
/
Peptidyl Transferases
/
Escherichia coli Proteins
/
Serine-Type D-Ala-D-Ala Carboxypeptidase
/
Escherichia coli
/
Hexosyltransferases
Language:
En
Year:
1991
Type:
Article