Sequence of the lye gene encoding the autolytic lysozyme of Clostridium acetobutylicum ATCC824: comparison with other lytic enzymes

doi:10.1016/0378-1119(91)90460-S

Gene

Volume 104, Issue 1, 31 July 1991, Pages 25-31

https://doi.org/10.1016/0378-1119(91)90460-S Get rights and content

Abstract

The lyc gene, encoding an autolytic lysozyme from Clostridium acetobutylicum ATCC824, has been cloned. The nucleotide sequence of the lyc gene has been determined and found to encode a protein of 324 amino acids (aa) with a deduced M_r of 34939. The lyc gene is preceded by two open reading frames with unknown functions, suggesting that this gene is part of an operon. Comparison between the deduced aa sequence of the lyc gene and the directly determined N-terminal sequence of the extracellular clostridial lysozyme suggests that the enzyme is synthesized without a cleavable signal peptide. Moreover, the comparative analyses between the clostridial lysozyme and other known cell-wall lytic enzymes revealed a significant similarity with the N-terminal portion of the lysozymes of Streptomyces globisporus, the fungus Chalaropsis, the Lactobacillus bulgaricus bacteriophage mvl, and the Streptococcus pneumoniae bacteriophages of the Cp family (CPL lysozymes). In addition, the analyses showed that the C-terminal half of the clostridial lysozyme was homologous to the N-terminal domain of the muramoyl-pentapeptide-carboxypeptidase of Streptomyces albus, suggesting a role in substrate binding. The existence of five putative repeated motifs in the C-terminal region of the autolytic lysozyme suggests that this region could play a role in the recognition of the polymeric substrate.

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It has become evident that several of the strains of Clostridium acetobutylicum that have been employed in physiological studies of the acetone-butanol fermentation, are heterogeneous. Studies of the phenotypic and genotypic characteristics of several of these strains (involving inter alia both pyrolysis mass spectrometry and 16S rRNA sequence determinations) demonstrated that the type strain obtained from ATCC was not identical with that supplied by NCIMB, and that NCIMB 8052T is in fact Clostridium beijerinckii. We therefore suggest that the name Clostridium acetobutylicum should be restricted to those strains that are genetically closely related to ATCC 824T (which include strains DSM 792 and DSM 1731 but not strain P262).
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Sequence of the lye gene encoding the autolytic lysozyme of Clostridium acetobutylicum ATCC824: comparison with other lytic enzymes

Abstract

Gene

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

Gene

Gene

Gene

FEMS Microbiol. Rev.

Gene

Gene

Autolytic activity and autolysis-deficient mutant of Clostridium acetobutylicum

Appl. Environ. Microbiol.

Effects of butanol on Clostridium acetobutylicum

Appl. Environ. Microbiol.

Cloning and expression of Clostridium acetobutylicum phosphotransbutyrylase and butyrate kinase genes in Escherichia coli

J. Bacteriol.

Purification and characterization of the extracellular lytic enzyme of Clostridium acetobutylicum ATCC824: a novel muramidase acting on non N-acetylated peptidoglycan

Appl. Environ. Microbiol.

Taxonomy of the Clostridia: wall composition and DNA homologies in Clostridium butyricum and other acid-producing clostridia

J. Gen. Microbiol.

Chimeric phage-bacterial enzymes, a clue in the molecular evolution of genes

Chimeric pneumococcal cell wall lytic enzymes reveal important physiological evolutionary traits

J. Biol. Chem.

Structure of a Zn2+-containing d-alanyl-d-alanine-cleaving carboxypeptidase at 2.5 Å resolution

Nature

Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages

Identification of a lytic enzyme of Clostridium acetobutylicum that degrades choline-containing pneumococcal cell walls

FEMS Microbiol. Lett.

Nucleotide sequence of Bacillus bacteriophage φ29 genes 14 and 15: homology of gene 15 with other bacteriophage lysozymes

Nucleic Acids Res.

Sequence of the cellulase gene of Clostridium thermocellum coding for endoglucananse B

Nucleic Acids Res.

Structure of a Zn²⁺-containing d-alanyl-d-alanine-cleaving carboxypeptidase at 2.5 Å resolution