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Antimicrobial Agents and Chemotherapy, February 2004, p. 484-490, Vol. 48, No. 2
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.2.484-490.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The ybxI Gene of Bacillus subtilis 168 Encodes a Class D ß-Lactamase of Low Activity

Maria-Luigi Colombo,1 Sophie Hanique,1 Stéphane L. Baurin,1 Cédric Bauvois,1 Kris De Vriendt,2 Jozef J. Van Beeumen,2 Jean-Marie Frère,1 and Bernard Joris1*

Centre d'Ingénierie des Protéines, Institut de Chimie B6a, Université de Liège, Sart Tilman, B-4000 Liège 1,1 Laboratorium voor Eiwitbiochemie en Eiwitengineering, Universiteit Gent, B-9000 Ghent, Belgium2

Received 28 March 2003/ Returned for modification 7 July 2003/ Accepted 25 September 2003

The ybxI gene of Bacillus subtilis 168 encodes a preprotein of 267 amino acid residues, including a putative signal peptide of 23 residues. The YbxI primary structure exhibits high similarity scores with two members of the superfamily of the serine penicillin-recognizing enzymes: the class D ß-lactamases and the hydrophilic carboxy-terminal domains of the BlaR and MecR penicillin receptors. To determine the function and the activity of this putative penicillin-recognizing enzyme, we have subcloned the ybxI gene in the pET-26b expression vector. Transformation of Escherichia coli BL21(DE3) by the recombinant plasmid pCIP51 resulted in the export of the mature YbxI in the periplasm as a water-soluble protein. The recombinant protein was purified to 95% homogeneity. YbxI interacts with several ß-lactam antibiotics and can hydrolyze some of them. YbxI is not inactivated by clavulanic acid. The YbxI function and its enzymatic activity in B. subtilis remain unknown. The acyl-enzyme obtained after incubation of YbxI with a fluorescent derivative of ampicillin can be detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, confirming that YbxI can be acylated by ß-lactam antibiotics. YbxI does not hydrolyze some of the standard substrates of D-alanyl-D-alanine peptidases, the targets of penicillin. YbxI belongs to the penicillin-recognizing enzyme family but has an activity intermediate between those of a penicillin-binding protein and a ß-lactamase.

* Corresponding author. Mailing address: Centre d'Ingénierie des Protéines, Institut de Chimie B6a, Université de Liège, Sart Tilman, B-4000 Liège, Belgium. Phone: (32) 4 366 29 54. Fax: (32) 4 366 33 64. E-mail: bjoris{at}ulg.ac.be.

Antimicrobial Agents and Chemotherapy, February 2004, p. 484-490, Vol. 48, No. 2
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.2.484-490.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Girlich, D., Leclercq, R., Naas, T., Nordmann, P. (2007). Molecular and Biochemical Characterization of the Chromosome-Encoded Class A {beta}-Lactamase BCL-1 from Bacillus clausii. Antimicrob. Agents Chemother. 51: 4009-4014 [Abstract] [Full Text]  
  • Jacoby, G. A. (2006). {beta}-Lactamase Nomenclature.. Antimicrob. Agents Chemother. 50: 1123-1129 [Full Text]  


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