Molecular characterization of the xerC gene of Lactobacillus leichmannii encoding a site-specific recombinase and two adjacent heat shock genes.

Abstract

Sequencing of four overlapping DNA fragments comprising 3.527 kb isolated from a L. leichmannii genomic library revealed three complete open reading frames (ORFs) and one that was truncated. The deduced amino acid sequences of the complete ORFs showed considerable similarities with the already known sequences of the xerC, hslV, and hslU gene products of Escherichia coli: the site-specific XerC recombinase, a member of the lambda integrase family, and the HtpI resp. HtpO heat shock proteins. The deduced amino acid sequence of the fourth, incomplete ORF upstream the xerC gene showed strong homology with the gid A gene product of B. subtilis.

• Authors: J Becker, M Brendel
• Journal: Current microbiology (Curr Microbiol) Vol. 32 Issue 4 Pg. 232-6 (Apr 1996) ISSN: 0343-8651 [Print] United States
• PMID: 8867465 (Publication Type: Journal Article)

Chemical References

• DNA, Bacterial
• Escherichia coli Proteins
• Heat-Shock Proteins
• Recombinases
• XerC protein, E coli
• DNA Nucleotidyltransferases
• Integrases
• integron integrase IntI1

Topics

• Amino Acid Sequence
• DNA Nucleotidyltransferases (genetics)
• DNA, Bacterial (genetics)
• Escherichia coli Proteins
• Genes, Bacterial
• Heat-Shock Proteins (genetics)
• Integrases
• Lactobacillus (enzymology, genetics)
• Molecular Sequence Data
• Open Reading Frames
• Recombinases
• Restriction Mapping
• Sequence Homology, Amino Acid