Abstract
We have purified a minor extracellular serine protease from Bacillus subtilis. Characterization of this enzyme indicated that it was most likely the previously reported enzyme bacillopeptidase F. The amino-terminal sequence of the purified protein was determined, and a "guess-mer" oligonucleotide hybridization probe was constructed on the basis of that sequence. This probe was used to identify and clone the structural gene (bpr) for bacillopeptidase F. The deduced amino acid sequence for the mature protein (496 amino acids) was preceded by a putative signal sequence of 30 residues and a putative propeptide region of 164 amino acids. The bpr gene mapped near pyrD on the chromosome and was not required for growth or sporulation.
MeSH Terms
Amino Acid Sequence
Bacillus subtilis/enzymology,genetics
Base Sequence
Blotting, Southern
Chromatography, Affinity
Chromatography, High Pressure Liquid
Chromosome Mapping
Chromosomes, Bacterial
Cloning, Molecular
Genes, Bacterial
Genotype
Kinetics
Molecular Sequence Data
Nucleic Acid Hybridization
Oligonucleotide Probes
Plasmids
Restriction Mapping
Sequence Homology, Nucleic Acid
Serine Endopeptidases/genetics,isolation & purification,metabolism
Chemicals
Oligonucleotide Probes
Serine Endopeptidases
bacillopeptidase F
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Sloma A
BioTechnica International, Inc., Cambridge, Massachusetts 02140.
Rufo G A
Rudolph C F
Sullivan B J
Theriault K A
Pero J
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