The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease
Abstract
The nucleotide sequence of wprA, a protease-encoding gene of Bacillus subtilis 168, is reported. The gene, expressed during the exponential growth phase, belongs to a monocistronic operon. WprA is a 96 kDa polypeptide endowed with a signal peptide, as well as a propeptide. Upon processing and export, it gives rise to two previously identified cell-wall-bound proteins, CWBP23 and 52. Processing of WprA exhibits a novel feature of protein export, whereby removal of the middle part of the molecule accompanies the targeting to the cell wall of its N- and C-terminal parts, which correspond to CWBP23 and 52, respectively. Sequence analyses and enzymic assays reveal that CWBP52 is a serine protease. Growth rate, cell morphology, sporulation and motility of wprA mutants apparently do not differ from those of the parent strain.
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“Taken together, our results suggest that the mechanism of PrtB attachment to the cell wall probably implicates electrostatic forces, as was proposed for WprA, a cell wall-associated protease of Bacillus subtilis (24).”
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Items 101–107 of 107
PrsA LIPOPROTEIN AND POSTTRANSLOCATIONAL FOLDING OF SECRETORY PROTEINS IN BACILLUS SUBTILIS
Vitikainen, M. (2004) · STM:n Hallinnonalan avoin julkaisuarkisto (Julkari)
“Identification and functions of type I signal peptidases of Bacillus amyloliquefaciens”
Fakultät, M.-N.-T., & Chu, V. H. H. (2015)
Proteome-wide analysis of the functional roles of bacilysin biosynthesis in Bacillus subtilis
Özcengiz, G., Taşkin, A. A., Demir, M., & Karataş, A. Y. (2014) · New Biotechnology · doi:10.1016/j.nbt.2014.05.1768
Characterization of the Bacillus subtilis Penicillin-Binding Protein PBP4
Broeck, A. V., Sauvage, E., Joris, B., & Duez, C. (2019) · Advances in Microbiology · doi:10.4236/aim.2019.93013
“subtilis cell walls bearing teichoic acids [18] and after subtraction of the amount of D-alanine measured in the blank, 6.”
Li, X., Wei, Z., Ge, J., Pan, Y., Chu, X., Huang, B., Zhao, J., Li, Y., & Zhou, Y. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.30.547221
“Except for the cell wall105 associated protease (WprA) (25), the remaining proteases are secreted into the growth 106 medium, potentially supplying an opportunity to efficiently degrade SP by using the 107 cultivation supernatant of B.”
BackgroundCavallarin, N. (2011) · Padua Research Archive (University of Padova)
Tan, G. C. (2013) · Swinburne figshare (Swinburne University of Technology) · doi:10.25916/sut.26288959
Metadata
- Authors
- Margot, P., & Karamata, D.
- Affiliations
- University of Lausanne (CH)
- Corresponding author
- Karamata, D.
- Venue
- Microbiology
- Publisher
- Microbiology Society
- Published
- 1996-12-01
- Volume
- 142
- Issue
- 12
- Pages
- 3437-3444
- ISSN
- 1350-0872 (ISSN-L)
- 1465-2080
- OpenAlex
- W2119045079
- Cited by
- 107
- References
- 36
- Citations by year
- 2023: 2 · 2022: 2 · 2021: 2 · 2020: 5 · 2019: 5 · 2018: 2 · 2017: 3 · 2016: 3 · 2015: 4 · 2014: 5 · 2013: 5 · 2012: 3
- FWCI
- 3.20
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Microbiology (publishedVersion)
- PubMed (publishedVersion)
- IRIS (submittedVersion)
- SERVAL (Université de Lausanne) (submittedVersion)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- Bacillus subtilis 168, serine protease, protein export, signal peptide, propeptide processing, exponential growth, gene sequence
- MeSH terms
- Amino Acid Sequence, Bacillus subtilis, Bacterial Proteins, Base Sequence, Binding Sites, Cell Wall, Cloning, Molecular, Genes, Bacterial, Molecular Sequence Data, Operon, Endopeptidases, Recombinant Proteins, Serine Endopeptidases, Subtilisins, Restriction Mapping, Gene Expression Regulation, Bacterial, Gene Expression Regulation, Enzymologic, Conserved Sequence, Sequence Homology, Amino Acid
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