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Literature summary extracted from

  • Zhou, R.; Kroos, L.
    Serine proteases from two cell types target different components of a complex that governs regulated intramembrane proteolysis of pro-sigmaK during Bacillus subtilis development (2005), Mol. Microbiol., 58, 835-846.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.B49 expressed as His-tag fusion protein in Escherichia coli Bacillus subtilis
3.4.21.116 expressed as His-tag fusion protein in Escherichia coli BL21(DE3) Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.B49 S309A inactive Bacillus subtilis
3.4.21.116 S378A unable to process self cleavage, unable to trigger the activation of pro-sigmaK processing Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.B23 BofA inhibition possibly by blocking the active site and providing a metal ligand Bacillus subtilis
3.4.24.B23 additional information inactive when bound to SpoIVFA and BofA, both proteins required for complete inhibition Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.B49 additional information secreted by the mother cell into the intermembrane space between the forespore and the mother cell membrane Bacillus subtilis
-
-
3.4.21.116 endospore-forming forespore secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane Bacillus subtilis 42601
-
3.4.24.B23 membrane
-
Bacillus subtilis 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B23 additional information metalloprotease Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.B49 BofA + H2O Bacillus subtilis involved in sigmaK signaling, acts in cooperation with SpoIVB, substrate and enzyme coexpressed in Escherichia coli, cleavage site near the C-terminus fragments of BofA
-
?
3.4.21.B49 additional information Bacillus subtilis autoproteolysis as observed for SpoIVB ?
-
?
3.4.21.B49 additional information Bacillus subtilis no effect on SpoIVFA when coexpressed in Escherichia coli ?
-
?
3.4.21.B49 additional information Bacillus subtilis PV79 autoproteolysis as observed for SpoIVB ?
-
?
3.4.21.B49 additional information Bacillus subtilis PV79 no effect on SpoIVFA when coexpressed in Escherichia coli ?
-
?
3.4.21.B49 additional information Bacillus subtilis PY79 autoproteolysis as observed for SpoIVB ?
-
?
3.4.21.B49 additional information Bacillus subtilis PY79 no effect on SpoIVFA when coexpressed in Escherichia coli ?
-
?
3.4.21.116 additional information Bacillus subtilis BofA is unsuitable as a substrate ?
-
?
3.4.21.116 additional information Bacillus subtilis self cleavage ?
-
?
3.4.21.116 additional information Bacillus subtilis PV79 BofA is unsuitable as a substrate ?
-
?
3.4.21.116 additional information Bacillus subtilis PV79 self cleavage ?
-
?
3.4.21.116 additional information Bacillus subtilis PY79 BofA is unsuitable as a substrate ?
-
?
3.4.21.116 additional information Bacillus subtilis PY79 self cleavage ?
-
?
3.4.21.116 SpoIVFA + H2O Bacillus subtilis involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
-
?
3.4.21.116 SpoIVFA + H2O Bacillus subtilis PV79 involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
-
?
3.4.21.116 SpoIVFA + H2O Bacillus subtilis PY79 involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
-
?
3.4.24.B23 pro-sigmaK + H2O Bacillus subtilis involved in the sporulation process sigmaK + peptide
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.B49 Bacillus subtilis
-
-
-
3.4.21.B49 Bacillus subtilis PY79
-
-
-
3.4.21.116 Bacillus subtilis
-
-
-
3.4.21.116 Bacillus subtilis PY79
-
-
-
3.4.24.B23 Bacillus subtilis
-
-
-
3.4.24.B23 Bacillus subtilis PV79
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.B49 BofA + H2O involved in sigmaK signaling, acts in cooperation with SpoIVB, substrate and enzyme coexpressed in Escherichia coli, cleavage site near the C-terminus Bacillus subtilis fragments of BofA
-
?
3.4.21.B49 GFP-delta27 BofA + H2O
-
Bacillus subtilis ? one or two low molecular weight species detected ?
3.4.21.B49 additional information autoproteolysis as observed for SpoIVB Bacillus subtilis ?
-
?
3.4.21.B49 additional information no effect on SpoIVFA when coexpressed in Escherichia coli Bacillus subtilis ?
-
?
3.4.21.B49 additional information autoproteolysis as observed for SpoIVB Bacillus subtilis PV79 ?
-
?
3.4.21.B49 additional information no effect on SpoIVFA when coexpressed in Escherichia coli Bacillus subtilis PV79 ?
-
?
3.4.21.B49 additional information autoproteolysis as observed for SpoIVB Bacillus subtilis PY79 ?
-
?
3.4.21.B49 additional information no effect on SpoIVFA when coexpressed in Escherichia coli Bacillus subtilis PY79 ?
-
?
3.4.21.116 additional information BofA is unsuitable as a substrate Bacillus subtilis ?
-
?
3.4.21.116 additional information self cleavage Bacillus subtilis ?
-
?
3.4.21.116 additional information BofA is unsuitable as a substrate Bacillus subtilis PV79 ?
-
?
3.4.21.116 additional information self cleavage Bacillus subtilis PV79 ?
-
?
3.4.21.116 additional information BofA is unsuitable as a substrate Bacillus subtilis PY79 ?
-
?
3.4.21.116 additional information self cleavage Bacillus subtilis PY79 ?
-
?
3.4.21.116 SpoIVFA + H2O involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing Bacillus subtilis cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
-
?
3.4.21.116 SpoIVFA + H2O involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing Bacillus subtilis PV79 cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
-
?
3.4.21.116 SpoIVFA + H2O involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing Bacillus subtilis PY79 cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
-
?
3.4.24.B23 pro-sigmaK + H2O involved in the sporulation process Bacillus subtilis sigmaK + peptide
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.B49 CtpB PDZ-containing serine protease with similar organization as SpoIVB Bacillus subtilis
3.4.21.116 SpoIVB
-
Bacillus subtilis
3.4.24.B23 SPOIVFB member of the site-2 protease family of the intramembrane-cleaving proteases Bacillus subtilis