Information on EC 3.4.21.116 - SpoIVB peptidase

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The expected taxonomic range for this enzyme is: Bacillus subtilis

EC NUMBER
COMMENTARY hide
3.4.21.116
-
RECOMMENDED NAME
GeneOntology No.
SpoIVB peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-terminal cleavage of the pro-form of the sporulation protein sigmaK
show the reaction diagram
self-cleaves Val52-/-Asn53, Ala62-/-Phe63 and Val74-/-Thr75 at the N-terminus of SpoIVB
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
258282-12-1
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296241-18-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CtpB + H2O
?
show the reaction diagram
CtpB-His6 + H2O
?
show the reaction diagram
GFP-SpoIVFA + H2O
?
show the reaction diagram
His tagged extracellular domain of SpoIVFA + H2O
?
show the reaction diagram
pro-sigmaK
sigmaK + ?
show the reaction diagram
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
show the reaction diagram
SpoIIQ + H2O
?
show the reaction diagram
SpoIVFA + H2O
17 KDa fragment + 14 KDa fragment
show the reaction diagram
-
component of the pro-sigmaK processing complex, cleaves between residues 145 and 175
-
?
SpoIVFA + H2O
?
show the reaction diagram
-
intrinsic protein substrate
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptides of SpoIVFA
show the reaction diagram
additional information
?
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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
CtpB + H2O
?
show the reaction diagram
pro-sigmaK
sigmaK + ?
show the reaction diagram
-
enzyme is essential for intercompartmental signalling in the sigmaK-checkpoint, activates poteolytic processing of pro-sigmaK to its mature and active form sigmaK, function in formation of heat-resistant spores
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?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
show the reaction diagram
SpoIIQ + H2O
?
show the reaction diagram
SpoIVFA + H2O
?
show the reaction diagram
-
intrinsic protein substrate
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptides of SpoIVFA
show the reaction diagram
additional information
?
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
in vivo assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
SDS-PAGE
42000
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three predominant species of approximately 45000 Da, 43000 Da and 42000 Da after processing
43000
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three predominant species of approximately 45000 Da, 43000 Da and 42000 Da after processing
45000
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three predominant species of approximately 45000 Da, 43000 Da and 42000 Da after processing
45980
calculated from amino acid sequence
50000
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proenzyme, SDS-PAGE
52000
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S378A mutant, unprocessed proprotein
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Enzyme binds specifically to intrinsic protein BofA
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein using His-tag
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)
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expressed as His-tag fusion protein in Escherichia coli BL21(DE3) pLys
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3)
expression of wild-type and enzyme mutants in mutants strain BSL51 and R13
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functional expression of wild-type, and expression of amino acid exchange mutants in the mutant strain BSL51, lacking spoIVFA and spoIVFB genes, and in the mutant OR745, lacking gene spoIVFB
fusion protein with beta-galactosidase
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D137E
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site-directed mutagenesis, mutant is completely impaired in pro-sigmaK processing
D137H
mutant shows no remaining sporulation activity
D149N
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impaired self-cleavage, no pro-sigmaK processing
D213L
phenotype indistinguishable from wild type, normal spore formation, slight accumulation of the 50 kDa species
D240L
phenotype indistinguishable from wild type, normal spore formation
D242L
phenotype indistinguishable from null mutant, fails to trigger and sigmaK signaling and to form heat and lysozyme resistant spores, production of an unstable protein that is rapidly cleared by secondary proteolysis
D242N
phenotype indistinguishable from wild type, normal spore formation
D363L
phenotype indistinguishable from null mutant, fails to trigger and sigmaK signaling and to form heat and lysozyme resistant spores, self cleavage of enzyme appears to delayed by approximately 30 min, accumulation of the 50 kDa species
D363N
phenotype indistinguishable from wild type, normal spore formation
G114A
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self-cleavage and pro-sigmaK processing similar to wild-type enzyme
G114Q
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impaired self-cleavage, delayed pro-sigmaK processing
G126A
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self-cleavage and pro-sigmaK processing similar to wild-type enzyme
G126Q
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self-cleavage and pro-sigmaK processing similar to wild-type enzyme
G138A
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site-directed mutagenesis, slightly reduced activity
G139A
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site-directed mutagenesis, slightly reduced activity
G144A
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self-cleavage and pro-sigmaK processing similar to wild-type enzyme
G144A/N155D
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self-cleavage and pro-sigmaK processing similar to wild-type enzyme
G144Q
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self-cleavage and pro-sigmaK processing similar to wild-type enzyme
H236F
phenotype indistinguishable from null mutant, fails to trigger and sigmaK signaling and to form heat and lysozyme resistant spores
H236N
phenotype indistinguishable from null mutant, fails to trigger and sigmaK signaling and to form heat and lysozyme resistant spores, accumulation of the 50 kDa species
H394D
production of approximately 30% fewer spores than wild type, unable to germinate properly at 37°C
H43A
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site-directed mutagenesis, no activity
I42P
mutant shows increased sporulation activity
K321A
phenotype indistinguishable from wild type, normal spore formation
K387A
phenotype indistinguishable from wild type, normal spore formation, slight accumulation of the 50 kDa species
N122A
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site-directed mutagenesis, extremely low enzyme expression
N122D
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site-directed mutagenesis, extremely low enzyme expression
N122Q
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site-directed mutagenesis, unaltered activity, similar to wild-type
N129A
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site-directed mutagenesis, slightly reduced activity
N155D
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self-cleavage and pro-sigmaK processing similar to wild-type enzyme
N155Y
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self-cleavage and pro-sigmaK processing similar to wild-type enzyme
N290I
production of approximately 30% fewer spores than wild type, unable to germinate properly at 37°C
P132A
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site-directed mutagenesis, highly reduced enzyme activity
R185H
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self-cleavage and pro-sigmaK processing similar to wild-type enzyme
R185K
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self-cleavage and pro-sigmaK processing similar to wild-type enzyme
S378K
phenotype indistinguishable from null mutant, fails to trigger and sigmaK signaling and to form heat and lysozyme resistant spores, self cleavage of enzyme appears to delayed by approximately 30 min, accumulation of the 50 kDa species
T228A
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can signal processing of pro-sigmaK but is unable to complete its non-signalling function
S378A
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unable to process self cleavage, unable to trigger the activation of pro-sigmaK processing
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D137N
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mutant shows highly reduced sporulation activity
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D213L
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phenotype indistinguishable from wild type, normal spore formation, slight accumulation of the 50 kDa species
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D242L
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phenotype indistinguishable from null mutant, fails to trigger and sigmaK signaling and to form heat and lysozyme resistant spores, production of an unstable protein that is rapidly cleared by secondary proteolysis
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D242N
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phenotype indistinguishable from wild type, normal spore formation
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E44A
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mutant shows nearly no remaining sporulation activity
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H236F
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phenotype indistinguishable from null mutant, fails to trigger and sigmaK signaling and to form heat and lysozyme resistant spores
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H236N
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phenotype indistinguishable from null mutant, fails to trigger and sigmaK signaling and to form heat and lysozyme resistant spores, accumulation of the 50 kDa species
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H43F
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mutant shows no remaining sporulation activity, no immunologically detectable enzyme protein
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I42P
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mutant shows increased sporulation activity
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S378A
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unable to process self cleavage, unable to trigger the activation of pro-sigmaK processing
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additional information
Show AA Sequence (188 entries)
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