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 Kohlbrecher, D Articles by Hengstenberg, W Search for Related Content PubMed PubMed Citation Articles by Kohlbrecher, D Articles by Hengstenberg, W

 Previous Article  |  Next Article 

J Bacteriol. 1992 April; 174(7): 2208-2214

research-article

Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system: molecular cloning and nucleotide sequence of the Staphylococcus carnosus ptsI gene and expression and complementation studies of the gene product.

Department of Microbiology, Ruhr-Universität Bochum, Germany.

ABSTRACT

A digoxigenin-labeled DNA probe that was complementary to the gene ptsH and the beginning of the gene ptsI was used to clone a 3.2-kb HincII-BamHI restriction fragment containing the complete ptsI gene of Staphylococcus carnosus. The restriction fragment was cloned in the antisense orientation to the lac promoter in the low-copy-number vector pSU18. The nucleotide sequences of the ptsI gene, which encodes enzyme I (EC 2.7.3.9), and the corresponding flanking regions were determined. The primary translation product, derived from the nucleotide sequence, consists of 574 amino acids and has a calculated molecular weight of 63,369. Amino acid sequence comparison showed 47% similarity to enzyme I of Escherichia coli and 37% similarity to the enzyme I domain of the multiphosphoryl transfer protein of Rhodobacter capsulatus. The histidinyl residue at position 191 could be identified as the probable phosphoenolpyruvate-dependent phosphorylation site of enzyme I of S. carnosus because of sequence homologies with the peptide sequences of enzyme I-active sites of Enterococcus faecalis and Lactococcus lactis. Several in vivo and in vitro complementation studies with the enzyme I ptsI genes of S. carnosus and the E. coli ptsI mutant JLT2 were carried out. The generation times and interaction between enzyme I with histidine-containing protein from gram-positive and gram-negative bacteria were measured in a phosphoryl group transfer test.

This article has been cited by other articles:

• Marquez, JoseA., Reinelt, S., Koch, B., Engelmann, R., Hengstenberg, W., Scheffzek, K. (2006). Structure of the Full-length Enzyme I of the Phosphoenolpyruvate-dependent Sugar Phosphotransferase System. J. Biol. Chem. 281: 32508-32515 [Abstract] [Full Text]  
• Luesink, E. J., Beumer, C. M. A., Kuipers, O. P., De Vos, W. M. (1999). Molecular Characterization of the Lactococcus lactis ptsHI Operon and Analysis of the Regulatory Role of HPr. J. Bacteriol. 181: 764-771 [Abstract] [Full Text]  
• Monedero, V., Postma, P. W., Pérez-Martínez, G. (1998). Suppression of the ptsH Mutation in Escherichia coli and Salmonella typhimurium by a DNA Fragment from Lactobacillus casei. J. Bacteriol. 180: 5247-5250 [Abstract] [Full Text]