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Cited by 144Probiotics and Fermented FoodsBacterial Genetics and BiotechnologyBiochemical and Structural Characterization

The DOI matches its Crossref record; 82 of the 82 references it cites were found in a registry or an index.

Multi-domain, cell-envelope proteinases of lactic acid bacteria.

Siezen, Roland J.·1999·Antonie van Leeuwenhoek
DOI 10.1023/a:1002036906922
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Abstract

The multi-domain, cell-envelope proteinases encoded by the genes prtB of Lactobacillus delbrueckii subsp. bulgaricus, prtH of Lactobacillus helveticus, prtP of Lactococcus lactis, scpA of Streptococcus pyogenes and csp of Streptococcus agalactiae have been compared using multiple sequence alignment, secondary structure prediction and database homology searching methods. This comparative analysis has led to the prediction of a number of different domains in these cell-envelope proteinases, and their homology, characteristics and putative function are described. These domains include, starting from the N-terminus, a pre-pro-domain for secretion and activation, a serine protease domain (with a smaller inserted domain), two large middle domains A and B of unknown but possibly regulatory function, a helical spacer domain, a hydrophilic cell-wall spacer or attachment domain, and a cell-wall anchor domain. Not all domains are present in each cell-envelope proteinase, suggesting that these multi-domain proteins are the result of gene shuffling and domain swapping during evolution.

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Crossref · 10.1023/a:1002036906922

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82 of 82 references verified0 citation errors · 0 not checkable

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  • Lactococcal PrtP proteinases are characterized by a signal sequence at the N-terminus that is cleaved during secretion across the membrane, and a LPXTG sorting motif followed by a hydrophobic membrane-spanning region and a positively charged tail at the C-terminus.

    “Like other CWAP, the lactococcal PrtP proteinases are characterized by a signal sequence at the N-terminus that is cleaved during secretion across the membrane; and a LPXTG sorting motif followed by a hydrophobic membrane-spanning region and a positively charged tail at the C-terminus [25].”

    From Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci (2007) · cites this paper as [25]

  • The cell envelope proteinase (CEP) of Lactococcus lactis is a large extracellular protease covalently linked to the peptidoglycan of the cell wall.

    “The cell envelope proteinase (CEP) of Lactococcus lactis is a large extracellular protease covalently linked to the peptidoglycan of the cell wall.”

    From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Siezen, 1999

  • The first 520 amino acid region has previously been recognized as the protease domain with homology to subtilisin.

    “This region has previously been recognized as the protease domain with homology to subtilisin (Siezen, 1999).”

    From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Siezen, 1999

  • The domain between residue 1570 and 1800 was termed the H-domain by Siezen due to the predicted helical secondary structure.

    “The domain between residue 1570 and 1800 was termed the H-domain by Siezen due to the predicted helical secondary structure (Siezen, 1999).”

    From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Siezen, 1999

  • Four of the six models extend beyond the catalytic domain and cover the A domain as defined by Siezen, and the Phyre2 structure extends well into the B domain before turning into an unstructured leash.

    “Four of the six models described in section “The proteinase domain” extends beyond the catalytic domain and covers also the A domain as defined by Siezen (1999) and the Phyre2 structure extends well into the B domain before turning into an unstructured leash.”

    From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Siezen, 1999

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 7

  1. De Vos WM & Siezen RJ (1994) Engineering pivotal proteins for lactococcal proteolysis. In: Andrews AT & Varley J (Eds) Biochemistry of Milk Products, Royal Society of Chemistry, Cambridge, UK, pp. 56-71
  2. Fischetti VA, Pancholi V & Schneewind O (1991) Common characteristics of the surface proteins from gram-positive cocci. In: Dunny GM, Cleary PP & McKay LL (Eds) Genetics and Molecular Biology of Streptococci, Lactococci, and Enterococci, American Society for Microbiol., pp. 290-294
  3. Hardie JM & Wiley RA (1994) The genus Streptococcus. In: Wood BJB & Holzapfel WH (Eds) The Lactic Acid Bacteria vol. 2, The Genera of Lactic Acid Bacteria, Blackie Academic and Professional, London, pp. 55-124
  4. King RD & Sternberg MJE (1999) Identification and application of concepts important for accurate and reliable protein secondary structure prediction. Protein Science, in press
  5. Laloi P, Atlan D, Blanc B, Gilbert C & Portalier R (1991) Cell-wall associated proteinase of Lactobacillus delbrueckii subsp. bulgaricus CNRZ397: differential extraction, purification and properties of the enzyme. Appl. Environm. Microbiol. 36: 196-204
  6. Mills OE & Thomas TD (1981) Nitrogen sources for growth of lactic streptococci in milk. N.Z. J. Dairy Sci. Technol. 16: 43-55
  7. Ven WJM van de, Roebroek AJM, van Duijnhoven HLP (1993) Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases. Crit. Rev. Oncogenesis 4: 115-136

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Metadata

Authors
Siezen, R. J.
Affiliations
Nederlands Instituut Voor Zuivel Oonderzoek (NL)
Corresponding author
Siezen, Roland J.
ORCID
Siezen, Roland J.
Venue
Antonie van Leeuwenhoek
Publisher
Springer Science and Business Media LLC
Published
1999-11
Volume
76
Issue
1-4
Pages
139-155
ISSN
  • 0003-6072 (ISSN-L)
  • 1572-9699
DOI
10.1023/a:1002036906922
OpenAlex
W4296216849
Cited by
144
References
82
Citations by year
2026: 1 · 2025: 5 · 2024: 1 · 2023: 3 · 2022: 3 · 2021: 5 · 2020: 3 · 2019: 1 · 2018: 3 · 2017: 8 · 2016: 3 · 2015: 6 · 2014: 5 · 2013: 7 · 2012: 8
FWCI
12.65
Type
journal article
Language
en
Open access
closed
Licence
Locations
Antonie van Leeuwenhoek (publishedVersion)
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 › Molecular Biology › Biochemical and Structural Characterization
Keywords
cell envelope proteinase, multidomain proteins, lactic acid bacteria, Lactobacillus bulgaricus, Lactobacillus helveticus, Lactococcus lactis, Streptococcus pyogenes, Streptococcus agalactiae, PrtP, ScpA, CSP, protein domain prediction, serine protease domain, DNA shuffling, domain swapping, protein evolution

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