Information on EC 3.4.21.102 - C-terminal processing peptidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.4.21.102
-
RECOMMENDED NAME
GeneOntology No.
C-terminal processing peptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
216484-75-2
-
92480-11-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PCC 7120, ORF ALL1021
-
-
Manually annotated by BRENDA team
strain 1330, gene ctpA
Q8FYM8
SwissProt
Manually annotated by BRENDA team
strain 1330, gene ctpA
Q8FYM8
SwissProt
Manually annotated by BRENDA team
synonym Gliocladium roseum, anamorph of Bionectria ochrdeuca
-
-
Manually annotated by BRENDA team
synonym Gliocladium roseum, anamorph of Bionectria ochrdeuca
-
-
Manually annotated by BRENDA team
Cyanothece sp.
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cultivar Kasalath
-
-
Manually annotated by BRENDA team
putative stromal processing peptidase
SwissProt
Manually annotated by BRENDA team
biovar viciae
-
-
Manually annotated by BRENDA team
strain 6803
-
-
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
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala + H2O
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala + Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
show the reaction diagram
-
-
-
?
Ac-WARAAARAAARBAAB + H2O
?
show the reaction diagram
-
i.e. peptide BAS9
-
-
?
Ac-WARAAARAAARBGGB + H2O
?
show the reaction diagram
-
i.e. peptide BAS10
-
-
?
anti-sigma factor MucA + H2O
?
show the reaction diagram
Arc repressor + H2O
?
show the reaction diagram
-
C-terminal sequence: GRIGA, endoproteolyric cleavage
-
-
?
C-terminal 19 amino acids of preD1 protein + H2O
pre-peptide of D1 + oligomer of 11 amino acids
show the reaction diagram
-
replacement of Ala at the cleaving site by Gly, Val, Pro reduces the rate of proteolysis to 50, 30 and 0% of the control
-
?
Cab1R protein precursor + H2O
?
show the reaction diagram
-
-
-
-
?
Cab2R protein precursor + H2O
?
show the reaction diagram
-
-
-
-
?
cytochrome-b562-WVAAA + H2O
?
show the reaction diagram
-
cytochrome b562 with a C-terminal attachment, fast hydrolysis
-
-
?
cytochrome-b562-WVAAK + H2O
?
show the reaction diagram
-
cytochrome b562 with a C-terminal attachment, no hydrolysis
-
-
?
cytochrome-b562-WVAAV + H2O
?
show the reaction diagram
-
cytochrome b562 with a C-terminal attachment, slow hydrolysis
-
-
?
cytochrome-b562-WVAGA + H2O
?
show the reaction diagram
-
cytochrome b562 with a C-terminal attachment, slow hydrolysis
-
-
?
cytochrome-b562-WVAYA + H2O
?
show the reaction diagram
-
cytochrome b562 with a C-terminal attachment, fast hydrolysis
-
-
?
cytochrome-b562-WVLAA + H2O
?
show the reaction diagram
-
cytochrome b562 with a C-terminal attachment, fast hydrolysis
-
-
?
cytochrome-b562-WVQAA + H2O
?
show the reaction diagram
-
cytochrome b562 with a C-terminal attachment, slow hydrolysis
-
-
?
D1 polypeptide of photosystem II + H2O
?
show the reaction diagram
D1 protein + H2O
?
show the reaction diagram
D1 protein precursor + H2O
mature D1 protein + ?
show the reaction diagram
-
-
-
?
F-24 peptide + H2O
?
show the reaction diagram
maize preOEC17
OEC17 + presequence
show the reaction diagram
-
precursor of thylakoid lumen protein OEC17
-
?
membrane protein SpoIVFA + H2O
?
show the reaction diagram
NIpI protein + H2O
?
show the reaction diagram
P-24 peptide + H2O
?
show the reaction diagram
peptide substrate comprising the 24 C-terminal residues of spinach pre-D1 protein
-
-
?
pre-D1 protein + H2O
D1 protein + peptide
show the reaction diagram
-
catalyzes the conversion of the nascent pre-D1 (pD1) protein into the active form of D1 by cleaving the 9 C-terminal residues in spinach, required to maintain the function of the photosystem II complex
-
-
?
pre-LHCP protein + H2O
LHCP protein + transit peptide
show the reaction diagram
-
-
-
?
pre-RBCS protein + H2O
RBCS protein + transit peptide
show the reaction diagram
-
-
-
-
?
prePsbO + H2O
PsbO + presequence
show the reaction diagram
-
precursor of thylakoid lumen protein PsbO or OEC33
-
?
Protein + H2O
?
show the reaction diagram
ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit precursor + H2O
?
show the reaction diagram
-
-
-
-
?
SP-4 peptide + H2O
?
show the reaction diagram
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
variant of the lambda repressor + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
anti-sigma factor MucA + H2O
?
show the reaction diagram
-
the Prc protease degrades mutants forms of MucA, the enzyme activity does not affect alginate production in strains with wild-type MucA, but MucA22 mutants show the mucoid phenotype, overview
-
-
?
Cab1R protein precursor + H2O
?
show the reaction diagram
-
-
-
-
?
Cab2R protein precursor + H2O
?
show the reaction diagram
-
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
show the reaction diagram
D1 protein + H2O
?
show the reaction diagram
Q41376
C-terminal processing of D1 protein
-
-
?
membrane protein SpoIVFA + H2O
?
show the reaction diagram
O35002
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
-
-
?
NIpI protein + H2O
?
show the reaction diagram
-
processing of wild-type substrate and mutants lacking up to 11 amino acids of the C-terminus in vivo, a mutant NIpI protein lacking 12 C-terminal amino acids is not processed, overview, the enzyme activates the substrate
-
-
?
pre-D1 protein + H2O
D1 protein + peptide
show the reaction diagram
-
catalyzes the conversion of the nascent pre-D1 (pD1) protein into the active form of D1 by cleaving the 9 C-terminal residues in spinach, required to maintain the function of the photosystem II complex
-
-
?
pre-LHCP protein + H2O
LHCP protein + transit peptide
show the reaction diagram
Q40983
-
-
-
?
pre-RBCS protein + H2O
RBCS protein + transit peptide
show the reaction diagram
-
-
-
-
?
Protein + H2O
?
show the reaction diagram
ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit precursor + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
activation
CoCl2
-
activation
MnCl2
-
activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(5S)-SB 214357
-
penem inhibitor, 1 mM, complete loss of activty
iodoacetamide
-
10 mM, 27% inhibition
phenylmethylsulfonyl fluoride
-
2 mM, 15% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0044 - 0.0111
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
0.035
Ac-WARAAARAAARBAAB
-
-
-
0.05
Arc repressor
-
-
-
0.3
C-terminal 19 amino acids of preD1 protein
-
pH 7.7, 25°C
-
additional information
additional information
steady-state kinetics of recombinant and native enzymes using two different assay methods, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
Escherichia coli
-
wild-type enzyme, mutants V229Q, V229E
3.7
Ac-WARAAARAAARBAAB
Escherichia coli
-
-
-
0.19
Arc repressor
Escherichia coli
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Spinacia oleracea
-
IC values in the micromolar range found for the effective inhibitors
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000007 - 0.000015
purified recombinant CtpA, substrates P-24 or F-24 peptides
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
-
strong dependence on pH-value
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme is not detected in the cytoplasm or in the membrane
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37900
-
calculation from sequnce of cDNA
42500
Q8FYM8
x * 42500, about, sequence calculation
43700
-
x * 43700, predicted from amino acid sequence
47000
-
x * 47000, SDS-PAGE
50000
recombinant enzyme, gel filtration
74320
-
calculation from sequence of cDNA
75000 - 80000
-
the enzyme possesses an N-terminal domain, a PDZ domain and a C-terminal catalytic domain
78500
-
TspH6, enzyme protein with six additional His residues at the C-terminus, sedimentation equilibrium
82000
-
1 * 82000, SDS-PAGE
139000
-
calculated from amino acid sequence
SUBUNITS
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
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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
; crystal structure
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
treatment with more than 0.15% v/v Triton X-100 results in loss of enzyme activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 20 mM Tris-HCl, pH 7.9, 1 M imidazole, 0.5 M NaCl, 33% glycerol
-
4°C, prolonged storage, proteolytic cleavage into two fragments of 50000 and 25000 Da
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant protein
-
native enzyme from leaves by anion exchange chromatography, hydroxyapatite chromatography, and gel filtration, refolded recombinant His-tagged CtpA by nickel affinity chromatography with a poor yield of active enzyme
Ni-NTA affinity column chromatography and Superdex 75 gel filtration
-
partial
-
partially purified from spinach, recombinant protein from Escherichia coli using His-tag
-
recombinant His-tagged enzyme from Escherichia coli strains BL21(DE3)pLysS or B834(DE3) by nickel affinity chromatography and gel filtration
wild-type and mutant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
creation of non functional mutants by insertional mutagenesis, strains carrying the mutation are growth deficient, and more sensitive to desiccation and detergents than the wild type strain
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli S17.1 cells
-
expression in Escherichia coli; overexpression in Escherichia coli
-
expression in the non-nitrogen-fixing cyanobacterium Synechocystis sp. PCC 6803
Cyanothece sp.
expression of the His-tagged enzyme in Escherichia coli strains BL21(DE3)pLysS or B834(DE3)
gene ctpA, DNA and amino acid sequence determination and analysis, genomic organization and structure, complementation of the mutant strain 1330DELTActpa by expression of wild-type gene ctpA
Q8FYM8
gene ctpA, expression of His-tagged CtpA in Escherichia coli mainly in inclusion bodies
gene prc from three strains, DNA and amino acid sequence determination and analysis, prc is located in a gene cluster encoding an extreme stress response system composed of anti-sigma factor MucA, negative regulator MucB, and ECF alternative sigma factor AlgU, regulation, overview
-
ORFs SLL2008 and SLL2009 encoding the C- and N-terminal enzyme part, respectively, operon organization
-
overexpressed in Arabidopsis thaliana, expressed as His-tag fusion protein in Escherichia coli
-
sequence analysis
single gene, sequence analysis, expression analysis
O48870
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the ctpA gene encoding C-terminal processing protease is maximal upon exposure to conditions encountered during infection
-
hyperosmotic shock (0.5-1.5 M NaCl) and treatment with cadmium (0.01-0.1 mM) and lead (0.02-0.2 mM) do not affect the expression of prC
isoform cPsbA4 is exclusively expressed during nighttime
Cyanothece sp.
the mRNA expression of prC is up-regulated by oxidants (0.5 mM of H2O2 and 5 mM of menadione achieve a maximal effect after 20 min) and heat shock (maximal effect after 20 min at 33-37°C), most likely through the stress response element
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D369A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
D441A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
D441N
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
D505A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
E433A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
E449A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
G375A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
G376A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H19A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H203A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H34A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H553A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H60A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
K455A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
K455R
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
R371A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
R444A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S372A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S428A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S430A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S430C
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S432A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
T452A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
V229E
-
increased Km for 2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
V229Q
-
increased Km for 2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
E97Q
no enzymic activity, but binding of transit peptide is not disturbed
H94L
no enzymic activity, but binding of transit peptide is not disturbed
D149A
-
very little protein detectable, processing of D1 protein of photosystem II takes place
D253A
-
no processing of D1 protein of photosystem II
D376A
-
very little protein detectable, processing of D1 protein of photosystem II takes place
E316A
-
no processing of D1 protein of photosystem II
E316Q
-
no photoautotrophic growth of cells
K338A
-
no processing of D1 protein of photosystem II
K338H
-
no photoautotrophic growth of cells
K338R
-
no photoautotrophic growth of cells
R198A
-
very little protein detectable, processing of D1 protein of photosystem II takes place
R255A
-
no processing of D1 protein of photosystem II
R255H
-
no photoautotrophic growth of cells
S313A
-
no processing of D1 protein of photosystem II
V205M/G282C
mutations mimic Prochlorococcus marinus D1 protein in mutant background accumulating divinyl chlorophyll. Energy transfer in CP47 is interrupted in photosystem II containing divinyl chlorophylls. The V205M/G282C mutation does not recover the energy transfer pathway in CP47, instead, the mutation allows the excitation energy transfer from CP43 to CP47, which neighbors in the photosystem II dimer
L132M/L210M
-
crystallization data of selenomethionyl derivative
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
solubilization from inclusion bodies and refolding of recombinant His-tagged CtpA
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
drug development
the enzyme is a target for development of herbicides
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