A germination-specific spore cortex-lytic enzyme from Bacillus cereus spores: cloning and sequencing of the gene and molecular characterization of the enzyme.
A gene (sleB) encoding a 24-kDa germination-specific spore cortex-lytic enzyme, probably an N-acetylmuramyl-L-alanine amidase, was cloned from Bacillus cereus, and its nucleotide sequence was determined. It was indicated that the enzyme is produced as a 259-residue protein with a signal sequence of 32 residues and is present in dormant spores in its active form. Sulfhydryl reagents inactivated the enzyme, but mutation of a single cysteine of the protein, Cys-258, to Gly did not cause complete inactivation of the enzyme, suggesting that the residue does not function as the catalytic center of enzyme.
Moriyama
R
R
Department of Applied Biological Sciences, School of Agricultural Sciences, Nagoya University, Japan.
Kudoh
S
S
Miyata
S
S
Nonobe
S
S
Hattori
A
A
Makino
S
S
D000581:Amidohydrolases / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D001409:Bacillus cereus / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D008969:Molecular Sequence Data; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D013171:Spores, Bacterial; D013439:Sulfhydryl Reagents / Q000494:pharmacology
D001426:Bacterial Proteins; D004269:DNA, Bacterial; C101656:SleB protein, Bacillus; D013439:Sulfhydryl Reagents; D000581:Amidohydrolases; D009238:N-Acetylmuramoyl-L-alanine Amidase