Literature summary for 3.4.21.102 extracted from

Mastny, M.; Heuck, A.; Kurzbauer, R.; Heiduk, A.; Boisguerin, P.; Volkmer, R.; Ehrmann, M.; Rodrigues, C.D.; Rudner, D.Z.; Clausen, T.
CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in Bacillus subtilis (2013), Cell, 155, 647-658.

Search for more literature for 3.4.21.102

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	a peptide ligand, which copurifies and cocrystallizes with CtpB, is observed at the entrance of the protease tunnel near the catalytic triad, its binding to the PDZ domain stimulates the protease activity	Bacillus subtilis

Cloned(Commentary)

Cloned (Comment)	Organism
expression of the His-tagged enzyme in Escherichia coli strains BL21(DE3)pLysS or B834(DE3)	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, all CtpB crystals are grown at 19°C using sitting-drop vapor-diffusion method, X-ray diffraction structure determination and crystal structure analysis	Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
membrane protein SpoIVFA + H2O	Bacillus subtilis	sequenctial processing by the enzyme together with protease 4B. The 4FA regulatory protein is composed of a globular N-terminal domain, a transmembrane helix (residues 73-90), an unstructured linker region and a compact C-terminal domain (residues 160-255, LytM-like) extending into the intermembrane space. 4B/CtpB-mediated removal of 4FA residues 131-154 induces sK maturation	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O35002	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strains BL21(DE3)pLysS or B834(DE3) by nickel affinity chromatography and gel filtration	Bacillus subtilis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
membrane protein SpoIVFA + H2O	-	Bacillus subtilis	?	-	?
membrane protein SpoIVFA + H2O	sequenctial processing by the enzyme together with protease 4B. The 4FA regulatory protein is composed of a globular N-terminal domain, a transmembrane helix (residues 73-90), an unstructured linker region and a compact C-terminal domain (residues 160-255, LytM-like) extending into the intermembrane space. 4B/CtpB-mediated removal of 4FA residues 131-154 induces sK maturation	Bacillus subtilis	?	-	?

Subunits

Subunits	Comment	Organism
dimer	the CtpB protease is organized as a dimeric ring with the catalytic site burried within a tunnel, domain organization of CtpB, overview	Bacillus subtilis

Synonyms

Synonyms	Comment	Organism
CtpB	-	Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Bacillus subtilis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Bacillus subtilis

General Information

General Information	Comment	Organism
evolution	the enzyme CtpB belongs to the widespread family of PDZ-proteases	Bacillus subtilis
additional information	the CtpB protease is organized as a dimeric ring with the catalytic site burried within a tunnel. The PDZ domain controls access to the protease tunnel. Residues Ser309, Lys334, and Gln338 function as catalytic triad mediating cleavage of the 4FA substrate. A peptide ligand, which copurifies and cocrystallizes with CtpB, is observed at the entrance of the protease tunnel near the catalytic triad	Bacillus subtilis
physiological function	spore formation in Bacillus subtilis relies on a regulated intramembrane proteolysis pathway, involving the enzyme, that synchronizes mother-cell and forespore development. Activating protease CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation. Activation of the SpoIV RIP pathway is induced by the concerted activity of enzyme CtpB and a second signaling protease, SpoIVB. Molecular basis of this SpoIV transmembrane signaling, the enzyme resembles a minimal version of a self-compartmentalizing protease regulated by a unique allosteric mechanism, overview	Bacillus subtilis

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Release 2023.1 (January 2023)