A new cell surface proteinase: sequencing and analysis of the prtB gene from Lactobacillus delbruekii subsp. bulgaricus
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Investigation of the chromosomal region downstream of the lacZ gene from Lactobacillus delbrueckii subsp. bulgaricus revealed the presence of a gene (prtB) encoding a proteinase of 1,946 residues with a predicted molecular mass of 212 kDa. The deduced amino acid sequence showed that PrtB proteinase displays significant homology with the N termini and catalytic domains of lactococcal PrtP cell surface proteinases and is probably synthesized as a preproprotein. However, the presence of a cysteine near the histidine of the PrtB active site suggests that PrtB belongs to the subfamily of cysteine subtilisins. The C-terminal region strongly differs from those of PrtP proteinases by having a high lysine content, an imperfect duplication of 41 residues, and a degenerated sequence compared with the consensus sequence for proteins anchoring in the cell walls of gram-positive bacteria. Finally, the product of the truncated prtM-like gene located immediately upstream of the prtB gene seems too short to be involved in the maturation of PrtB.
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The carboxy end of PrtB was previously shown to be different from the consensus anchoring region of other CSPs and exhibits an imperfect duplication of 59 amino acids with a high lysine content.
“The carboxy end of PrtB was previously shown to be different from the consensus anchoring region of other CSPs and exhibits an imperfect duplication of 59 amino acids with a high lysine content.”
Four different types of genes encoding CSPs of dairy lactic acid bacteria have been cloned and sequenced: prtB from L. bulgaricus, prtP from Lactococcus lactis and Lactobacillus casei, prtS from Streptococcus thermophilus, and prtH from Lactobacillus helveticus.
“So far, four different types of genes encoding CSPs of dairy lactic acid bacteria have been cloned and sequenced: prtB from L. bulgaricus, prtP from Lactococcus lactis and Lactobacillus casei, prtS from Streptococcus thermophilus, and prtH from Lactobacillus helveticus (8, 13, 18, 21, 28, 38).”
PrtB of L. bulgaricus strongly differs from other CSPs in its specificity of cleavage and the structure of the long C-extension domains.
“The PrtB of L. bulgaricus strongly differs from other CSPs in its specificity of cleavage and the structure of the long C-extension domains (∼1,100 residues) (13, 23).”
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References 52 · Cited by 117
- Authors
- Gilbert, C., Atlan, D., Blanc, B., Portailer, R., Germond, J. E., Lapierre, L., & Mollet, B.
- Affiliations
- Lyon 1 Université (FR)
- ORCID
- Gilbert, C
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1996-06
- Volume
- 178
- Issue
- 11
- Pages
- 3059-3065
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC178052
- OpenAlex
- W1575325624
- Cited by
- 117
- References
- 52
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 2 · 2023: 4 · 2022: 4 · 2021: 4 · 2020: 4 · 2019: 2 · 2018: 2 · 2017: 3 · 2016: 3 · 2015: 6 · 2014: 5 · 2013: 3 · 2012: 7
- FWCI
- 9.79
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Journal of Bacteriology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Centre National de la Recherche Scientifique
- Université de Lyon
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Keywords
- Lactobacillus bulgaricus, preproprotein, cell wall anchoring, gene sequencing, amino acid sequence analysis
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, Base Sequence, Binding Sites, DNA, Bacterial, Genes, Bacterial, Lactobacillus, Membrane Proteins, Molecular Sequence Data, Endopeptidases, Serine Endopeptidases
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