This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Popham, D L Articles by Setlow, P Search for Related Content PubMed PubMed Citation Articles by Popham, D L Articles by Setlow, P

 Previous Article  |  Next Article 

J Bacteriol. 1993 May; 175(10): 2917-2925

research-article

Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpE operon, which codes for penicillin-binding protein 4* and an apparent amino acid racemase.

Department of Biochemistry, University of Connecticut Health Center, Farmington 06032.

ABSTRACT

Penicillin-binding protein 4* (PBP 4*) was purified from Bacillus subtilis, its N-terminal sequence was determined, and the coding gene, termed pbpE, was cloned and sequenced. The predicted amino acid sequence of PBP 4* exhibited similarity to those of other penicillin-recognizing enzymes. Downstream of pbpE there was a second gene, termed orf2, which exhibited sequence similarity with aspartate racemase. The two genes were found to constitute an operon adjacent to and divergently transcribed from the sacB gene at 296 degrees on the chromosomal map. A weak beta-lactamase activity was associated with PBP 4*, but no enzymatic activity was found for the product of orf2. Mutation of pbpE, orf2, or both genes resulted in no observable effect on growth, sporulation, spore heat resistance, or spore germination. A translational pbpE-lacZ fusion was weakly expressed during vegetative growth and was significantly induced at the onset of sporulation. This induction depended on the activity of the spo0A product in relieving repression by the abrB repressor. A single transcription start site which was apparently dependent on E sigma A was detected upstream of pbpE.

This article has been cited by other articles:

• Scheffers, D.-J., Pinho, M. G. (2005). Bacterial Cell Wall Synthesis: New Insights from Localization Studies. Microbiol. Mol. Biol. Rev. 69: 585-607 [Abstract] [Full Text]  
• Scheffers, D.-J. (2005). Dynamic localization of penicillin-binding proteins during spore development in Bacillus subtilis. Microbiology 151: 999-1012 [Abstract] [Full Text]  
• Zellmeier, S., Zuber, U., Schumann, W., Wiegert, T. (2003). The Absence of FtsH Metalloprotease Activity Causes Overexpression of the {sigma}W-Controlled pbpE Gene, Resulting in Filamentous Growth of Bacillus subtilis. J. Bacteriol. 185: 973-982 [Abstract] [Full Text]  
• Ffrench-Constant, R. H., Waterfield, N., Burland, V., Perna, N. T., Daborn, P. J., Bowen, D., Blattner, F. R. (2000). A Genomic Sample Sequence of the Entomopathogenic Bacterium Photorhabdus luminescens W14: Potential Implications for Virulence. Appl. Environ. Microbiol. 66: 3310-3329 [Abstract] [Full Text]  
• Atrih, A., Bacher, G., Allmaier, G., Williamson, M. P., Foster, S. J. (1999). Analysis of Peptidoglycan Structure from Vegetative Cells of Bacillus subtilis 168 and Role of PBP 5 in Peptidoglycan Maturation. J. Bacteriol. 181: 3956-3966 [Abstract] [Full Text]  
• Popham, D. L., Gilmore, M. E., Setlow, P. (1999). Roles of Low-Molecular-Weight Penicillin-Binding Proteins in Bacillus subtilis Spore Peptidoglycan Synthesis and Spore Properties. J. Bacteriol. 181: 126-132 [Abstract] [Full Text]  
• Pedersen, L. B., Murray, T., Popham, D. L., Setlow, P. (1998). Characterization of dacC, Which Encodes a New Low-Molecular-Weight Penicillin-Binding Protein in Bacillus subtilis. J. Bacteriol. 180: 4967-4973 [Abstract] [Full Text]  
• Murray, T., Popham, D. L., Setlow, P. (1998). Bacillus subtilis Cells Lacking Penicillin-Binding Protein 1 Require Increased Levels of Divalent Cations for Growth. J. Bacteriol. 180: 4555-4563 [Abstract] [Full Text]  
• Asano, Y., Ito, H., Dairi, T., Kato, Y. (1996). An Alkaline D-Stereospecific Endopeptidase with beta -Lactamase Activity from Bacillus cereus. J. Biol. Chem. 271: 30256-30262 [Abstract] [Full Text]