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Literature summary for 3.4.21.116 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
Search for more literature for 3.4.21.116

Cloned(Commentary)

Cloned (Comment) Organism
expressed as His-tag fusion protein in Escherichia coli BL21(DE3) Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
S378A unable to process self cleavage, unable to trigger the activation of pro-sigmaK processing Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
endospore-forming forespore secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane Bacillus subtilis 42601
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bacillus subtilis BofA is unsuitable as a substrate ?
-
 ?
additional information Bacillus subtilis self cleavage ?
-
 ?
additional information Bacillus subtilis PV79 BofA is unsuitable as a substrate ?
-
 ?
additional information Bacillus subtilis PV79 self cleavage ?
-
 ?
additional information Bacillus subtilis PY79 BofA is unsuitable as a substrate ?
-
 ?
additional information Bacillus subtilis PY79 self cleavage ?
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis PY79
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information BofA is unsuitable as a substrate Bacillus subtilis ?
-
 ?
additional information self cleavage Bacillus subtilis ?
-
 ?
additional information BofA is unsuitable as a substrate Bacillus subtilis PV79 ?
-
 ?
additional information self cleavage Bacillus subtilis PV79 ?
-
 ?
additional information BofA is unsuitable as a substrate Bacillus subtilis PY79 ?
-
 ?
additional information self cleavage Bacillus subtilis PY79 ?
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?

Synonyms

Synonyms Comment Organism
SpoIVB
-
 Bacillus subtilis