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Literature summary for 3.4.24.B23 extracted from

  • Zhou, R.; Cusumano, C.; Sui, D.; Garavito, R.M.; Kroos, L.
    Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP (2009), Proc. Natl. Acad. Sci. USA, 106, 16174-16179.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.B23

Activating Compound

Activating Compound Comment Organism Structure
ATP SpoIVFB activity requires ATP, which binds to the C-terminal cystathionine-beta-synthase domain of SpoIVFB. ATP probably regulates substrate access to the active site and renders cleavage sensitive to the cellular energy level Bacillus subtilis
additional information incorporation of SpoIVFB into preformed liposomes stimulates its ability to cleave pro-sigmaK Bacillus subtilis

Cloned(Commentary)

Cloned (Comment) Organism
expression of functional SpoIVFB protein with an extra transmembrane segment attached to the N-terminus in Escherichia coli, the modification results in 100fold increased expression rate and facilitated purification Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
E44Q site-directed mutagenesis of SpoIVFB protein with an extra transmembrane segment , the mutant is inactive with substrate mutant pro-sigmaK S20G in contrast to the wild-type enzyme Bacillus subtilis
additional information construction of SpoIVFB protein with an extra transmembrane segment attached to the N-terminus for increased expression rate and facilitated purification, overview. Deletion of 10 residues from the C-terminal end of SpoIVFB nearly eliminates cleavage of coexpressed pro-sigmaK in recombinant Escherichia coli Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
 Bacillus subtilis
additional information no inhibition by ethanol Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Bacillus subtilis 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required, the enzyme is a metalloprotease Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pro-sigmaK + H2O Bacillus subtilis SpoIVFB protein and SpoIVFB protein with an extra transmembrane segment cleave membrane-tethered pro-sigmaK, releasing sigmaK to direct transcription of genes necessary for spore formation. The CBS domain of SpoIVFB interacts with pro-sugmaK, and ATP changes the interaction, suggesting that ATP regulates substrate access to the active site and renders cleavage sensitive to the cellular energy level sigmaK + sigmaK propeptide
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pro-sigmaK + H2O
-
 Bacillus subtilis sigmaK + sigmaK propeptide
-
 ?
pro-sigmaK + H2O SpoIVFB protein and SpoIVFB protein with an extra transmembrane segment cleave membrane-tethered pro-sigmaK, releasing sigmaK to direct transcription of genes necessary for spore formation. The CBS domain of SpoIVFB interacts with pro-sugmaK, and ATP changes the interaction, suggesting that ATP regulates substrate access to the active site and renders cleavage sensitive to the cellular energy level Bacillus subtilis sigmaK + sigmaK propeptide
-
 ?
pro-sigmaK S20G + H2O the substrate mutant is cleaved by the SpoIVFB protein with an extra transmembrane segment, but not by its mutant E44Q Bacillus subtilis sigmaK S20G + sigmaK propeptide
-
 ?

Synonyms

Synonyms Comment Organism
SpoIVFB protein
-
 Bacillus subtilis

General Information

General Information Comment Organism
physiological function SpoIVFB protein cleaves membrane-tethered Pro-sigmaK, releasing sigmaK to direct transcription of genes necessary for spore formation Bacillus subtilis