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Information on EC 3.4.21.102 - C-terminal processing peptidase and Organism(s) Bacillus subtilis and UniProt Accession O35002

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.102 C-terminal processing peptidase
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Bacillus subtilis
UNIPROT: O35002 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
stromal processing peptidase, c-terminal protease, tail-specific protease, photosystem ii d1 protein, c-terminal processing protease, carboxyl-terminal processing protease, prc protein, carboxyl-terminal protease, photosystem ii protein d1, protease re, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-terminal processing peptidase
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C-terminal processing protease
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carboxy terminal-processing proteinase
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chloroplast protein precursor processing proteinase
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CtpA gene product
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D1 preprotein-processing proteinase
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D1 protein-processing enzyme
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photosystem D1 protein precursor carboxyl-terminal processing protease
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photosystem II D1 C-terminal processing protease
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photosystem II D1 protein
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photosystem II D1 protein processing proteinase
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PRC protein
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processing peptidase
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protease Re
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proteinase CtpA
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proteinase, chloroplast protein precursor-processing
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stromal processing peptidase
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tail-specific protease
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thylakoid protein precursor processing peptidase
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Tsp protease
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
216484-75-2
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92480-11-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
membrane protein SpoIVFA + H2O
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show the reaction diagram
Protein + H2O
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show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
membrane protein SpoIVFA + H2O
?
show the reaction diagram
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
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Protein + H2O
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show the reaction diagram
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme CtpB belongs to the widespread family of PDZ-proteases
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
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
the CtpB protease is organized as a dimeric ring with the catalytic site burried within a tunnel, domain organization of CtpB, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strains BL21(DE3)pLysS or B834(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the His-tagged enzyme in Escherichia coli strains BL21(DE3)pLysS or B834(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Keiler, K.C.; Sauer, R.T.
Tsp protease
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
460-461
1998
Bacillus subtilis, Bartonella bacilliformis, Escherichia coli, Haemophilus influenzae, Neisseria gonorrhoeae
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Manually annotated by BRENDA team
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
Cell
155
647-658
2013
Bacillus subtilis (O35002)
Manually annotated by BRENDA team