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
3.4.21.116
-
RECOMMENDED NAME
GeneOntology No.
SpoIVB peptidase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
N-terminal cleavage of the pro-form of the sporulation protein sigmaK
show the reaction diagram
enzyme belongs to S2P family of intramembrane-cleaving proteases
-
N-terminal cleavage of the pro-form of the sporulation protein sigmaK
show the reaction diagram
enzyme is a metalloprotease with a transmembrane H43EXXH47 motif, E44 promotes nucleophilic attack by a water molecule on the carbonyl atom of the substrate peptide bond
-
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
-
-
-
-
self-cleaves Val52-/-Asn53, Ala62-/-Phe63 and Val74-/-Thr75 at the N-terminus of SpoIVB
show the reaction diagram
enzyme contains conserved metalloprotease sequence motif HEXXH
P26937
self-cleaves Val52-/-Asn53, Ala62-/-Phe63 and Val74-/-Thr75 at the N-terminus of SpoIVB
show the reaction diagram
D137 is essential for catalytic activity, mechanism model, enzyme contains conserved metalloprotease sequence motifs HEXXH and NPDG, which are expected to form the catalytic center and are required for catalytic activity
-
self-cleaves Val52-/-Asn53, Ala62-/-Phe63 and Val74-/-Thr75 at the N-terminus of SpoIVB
show the reaction diagram
enzyme contains conserved metalloprotease sequence motif HEXXH
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
M50.002
-
Merops-ID
M50.002
P26937
Merops-ID
M50.002
P26937
Merops-ID
-
S55.001
-
Merops ID
SpoIVB
-
not identical with SpoIVFB
SpoIVB
P17896
-
SpoIVB
Bacillus subtilis PV79
-
;
-
SpoIVB
-
not identical with SpoIVFB
-
SpoIVB
P17896
-
-
SpoIVB serine peptidase
-
-
SpolVFB
P26937
-
SpolVFB
P26937
-
-
sporulation protein SpolVFB
-
-
-
-
stage IV sporulation protein FB
-
-
stage IV sporulation protein FB
P26937
-
stage IV sporulation protein FB
P26937
-
-
CAS REGISTRY NUMBER
COMMENTARY
258282-12-1
-
296241-18-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
; strain PY79
-
-
Manually annotated by BRENDA team
residues 187-425; strain PY79
SwissProt
Manually annotated by BRENDA team
strain PY79
SwissProt
Manually annotated by BRENDA team
wild-type strain PY79
-
-
Manually annotated by BRENDA team
residues 187-425; strain PY79
SwissProt
Manually annotated by BRENDA team
strain PY79
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CtpB + H2O
?
show the reaction diagram
-
-, activation of CtpB
-
-
?
CtpB + H2O
?
show the reaction diagram
-
cleavage is not required to activate CtpB protease activity
-
-
?
CtpB + H2O
?
show the reaction diagram
-
-, activation of CtpB
-
-
?
CtpB-His6 + H2O
?
show the reaction diagram
-
effective cleavage to a size similar to that observed during sporulation process
-
-
?
GFP-SpoIVFA + 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
-
?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
show the reaction diagram
-
-
-
-
?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
show the reaction diagram
-
processing of prosigmaK, which is a protein involved in sporulation
-
?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
show the reaction diagram
P26937
processing of prosigmaK, which is a protein involved in sporulation
-
?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
show the reaction diagram
-
amino acids 1-117 are required as a minimum for pro-sigmaK to serve as a substrate, amino acids 1-126 are cleaved much more efficiently. Substitution E13K in pro-sigmaK reduces accumulation of substrate and prevents cleavage by enzmye
-
-
?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
show the reaction diagram
-
amino acids 1-126 of substrate pro-sigmaK are sufficient to serve as a substrate
-
-
?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
show the reaction diagram
P26937
processing of prosigmaK, which is a protein involved in sporulation
-
?
SpoIIQ + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis PV79, Bacillus subtilis PY79
-
protein located in the forespore membrane, cleavage of the extracellular domain, involved in the regulation of sigmaK processing
-
-
?
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
-
involved in the regulation of sporulation, cleavage of the extracellular domain at multiple sides, cleavage is thought to cause a conformational change in the signaling complex that activates SpoIVFB-dependent pro-sigmaK processing, activity of SpoIVB is absolutely essential for sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain, absolutely essential for sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
P17896
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
Bacillus subtilis PV79
-
involved in the regulation of sporulation, cleavage of the extracellular domain, absolutely essential for sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
Bacillus subtilis PV79
-
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain, absolutely essential for sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain at multiple sides, cleavage is thought to cause a conformational change in the signaling complex that activates SpoIVFB-dependent pro-sigmaK processing, activity of SpoIVB is absolutely essential for sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
P17896
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptides of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA at multiple sites activates SpoIVFB which is the enzyme for pro-sigmaK processing, activation of SpoIVFB is suggested to result from conformational changes caused by SpoIVFA cleavage
-
-
?
His tagged extracellular domain of SpoIVFA + H2O
?
show the reaction diagram
-
four cleavage sites identified
-
-
?
additional information
?
-
-
self-cleavage occurs at three different sites: Val52 and Asn53, Ala62 and Phe63, Val74 and Thr75
-
?
additional information
?
-
-
critical component of the intercompartmental signal-transduction pathway that activates the sigma factor, sigmaK, in the mother cell of the sporulating cell, possible non-signalling function in germ cell wall biosynthesis and the formation of heat-resistant spores
-
?
additional information
?
-
-
enzyme is a critical component of the sigmaK regulatory checkpoint during spore formation, PDZ domain can interact with BofC
-
?
additional information
?
-
-
initiates proteolytic processing of pro-sigmaK to its mature and active form in the opposed mother cell chamber of the developing cell, interacts with BofC
-
?
additional information
?
-
-
autoproteolytical activation. PDZ domain of enzyme binds to enzyme N-terminus to maintain its zymogen form. Following secretion across a spore membrane, domain binds in trans to the C-terminus of another enzyme molecule thus facilitating first cleavage event of enzyme near the N-terminus which releases the enzyme from the forespore membrane
-
-
-
additional information
?
-
-
BofA is unsuitable as a substrate, self cleavage
-
-
-
additional information
?
-
P17896
self cleavage into at least three distinct species of 46, 45, and 44 kDa
-
-
-
additional information
?
-
Bacillus subtilis PV79
-
BofA is unsuitable as a substrate, self cleavage
-
-
-
additional information
?
-
-
BofA is unsuitable as a substrate, self cleavage
-
-
-
additional information
?
-
P17896
self cleavage into at least three distinct species of 46, 45, and 44 kDa
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CtpB + H2O
?
show the reaction diagram
-
activation of CtpB
-
-
?
CtpB + H2O
?
show the reaction diagram
-
cleavage is not required to activate CtpB protease activity
-
-
?
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
-
?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
show the reaction diagram
-
-
-
-
?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
show the reaction diagram
-
processing of prosigmaK, which is a protein involved in sporulation
-
?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
show the reaction diagram
P26937
processing of prosigmaK, which is a protein involved in sporulation
-
?
SpoIIQ + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis PV79, Bacillus subtilis PY79
-
protein located in the forespore membrane, cleavage of the extracellular domain, involved in the regulation of sigmaK processing
-
-
?
SpoIVFA + H2O
?
show the reaction diagram
-
intrinsic protein substrate
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain at multiple sides, cleavage is thought to cause a conformational change in the signaling complex that activates SpoIVFB-dependent pro-sigmaK processing, activity of SpoIVB is absolutely essential for sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain, absolutely essential for sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
P17896
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptides of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA at multiple sites activates SpoIVFB which is the enzyme for pro-sigmaK processing, activation of SpoIVFB is suggested to result from conformational changes caused by SpoIVFA cleavage
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
Bacillus subtilis PV79
-
involved in the regulation of sporulation, cleavage of the extracellular domain, absolutely essential for sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
Bacillus subtilis PV79
-
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain, absolutely essential for sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain at multiple sides, cleavage is thought to cause a conformational change in the signaling complex that activates SpoIVFB-dependent pro-sigmaK processing, activity of SpoIVB is absolutely essential for sigmaK processing
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptides of SpoIVFA
show the reaction diagram
-
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA at multiple sites activates SpoIVFB which is the enzyme for pro-sigmaK processing, activation of SpoIVFB is suggested to result from conformational changes caused by SpoIVFA cleavage
-
-
?
SpoIVFA + H2O
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
show the reaction diagram
P17896
involved in the regulation of sporulation, cleavage of the extracellular domain, essential for sigmaK processing, cleavage of SpoIVFA activates SpoIVFB which is the enzyme for pro-sigmaK processing
-
-
?
CtpB + H2O
?
show the reaction diagram
-
activation of CtpB
-
-
?
additional information
?
-
-
critical component of the intercompartmental signal-transduction pathway that activates the sigma factor, sigmaK, in the mother cell of the sporulating cell, possible non-signalling function in germ cell wall biosynthesis and the formation of heat-resistant spores
-
?
additional information
?
-
-
enzyme is a critical component of the sigmaK regulatory checkpoint during spore formation, PDZ domain can interact with BofC
-
?
additional information
?
-
-
initiates proteolytic processing of pro-sigmaK to its mature and active form in the opposed mother cell chamber of the developing cell, interacts with BofC
-
?
additional information
?
-
-
autoproteolytical activation. PDZ domain of enzyme binds to enzyme N-terminus to maintain its zymogen form. Following secretion across a spore membrane, domain binds in trans to the C-terminus of another enzyme molecule thus facilitating first cleavage event of enzyme near the N-terminus which releases the enzyme from the forespore membrane
-
-
-
additional information
?
-
-
BofA is unsuitable as a substrate, self cleavage
-
-
-
additional information
?
-
P17896
self cleavage into at least three distinct species of 46, 45, and 44 kDa
-
-
-
additional information
?
-
Bacillus subtilis PV79
-
BofA is unsuitable as a substrate, self cleavage
-
-
-
additional information
?
-
-
BofA is unsuitable as a substrate, self cleavage
-
-
-
additional information
?
-
P17896
self cleavage into at least three distinct species of 46, 45, and 44 kDa
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
P26937
in vivo assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
during early engulfment, enzyme localizes to discrete foci at the septum and in traces at the mother cell cytoplasmic membrane. After fusion, there is a continuous accumulation in the outer forespore. Proteins SpoIIQ and SpoIIIAGH are required for correct localization of enzyme
Manually annotated by BRENDA team
Bacillus subtilis PV79, Bacillus subtilis PY79
-
during early engulfment, enzyme localizes to discrete foci at the septum and in traces at the mother cell cytoplasmic membrane. After fusion, there is a continuous accumulation in the outer forespore. Proteins SpoIIQ and SpoIIIAGH are required for correct localization of enzyme
-
Manually annotated by BRENDA team
-
during early engulfment, enzyme localize to discrete foci at the septum and in traces at the mother cell cytoplasmic membrane
-
Manually annotated by BRENDA team
Bacillus subtilis PV79, Bacillus subtilis PY79
-
during early engulfment, enzyme localize to discrete foci at the septum and in traces at the mother cell cytoplasmic membrane
-
-
Manually annotated by BRENDA team
-
secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane
Manually annotated by BRENDA team
Bacillus subtilis PV79
-
secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane; secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane
-
Manually annotated by BRENDA team
-
secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane; secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane; secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane; secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane; secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane
-
Manually annotated by BRENDA team
Bacillus subtilis PV79, Bacillus subtilis PY79
-
-
-
-
Manually annotated by BRENDA team
P26937
belongs to the family of putative membrane metalloproteases
Manually annotated by BRENDA team
-
catalytic center is located adjacent tot or within the membrane
Manually annotated by BRENDA team
-
belongs to the family of putative membrane metalloproteases
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
31000
-
-
SDS-PAGE
42000
-
-
three predominant species of approximately 45000 Da, 43000 Da and 42000 Da after processing
43000
-
-
three predominant species of approximately 45000 Da, 43000 Da and 42000 Da after processing
45000
-
-
three predominant species of approximately 45000 Da, 43000 Da and 42000 Da after processing
45980
-
P17896
calculated from amino acid sequence
50000
-
-
proenzyme, SDS-PAGE
52000
-
-
S378A mutant, unprocessed proprotein
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
P17896
synthesized as 50 kDa protein at about the second h of the sporulation process, starting at h three enzyme is cleaved into at least three distinct species of 46, 45, and 44 kDa, one of which is the active form of the enzyme, further processing into enzymatically inactive 42 and 40 kDa species
?
-
x * 46000, full-length protein, x * 40000, x * 39000, x * 38000, autoactivation products, SDS-PAGE
?
-
synthesized as 50 kDa protein at about the second h of the sporulation process, starting at h three enzyme is cleaved into at least three distinct species of 46, 45, and 44 kDa, one of which is the active form of the enzyme, further processing into enzymatically inactive 42 and 40 kDa species
-
additional information
-
Enzyme binds specifically to intrinsic protein BofA
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
self-cleavage releases its active form
proteolytic modification
-
enzyme is able to self-cleave in trans into at least three discrete products, zymogen is subject to two levels of proteolysis: autoproteolysis generating intermediate products of 42000 Da, 43000 Da and 45000 Da, at least one of which is proposed to be the active form, followed by processing by one or more enzymes to smaller species of 42000 Da and 40000 Da
proteolytic modification
-
autoproteolytical activation. PDZ domain of enzyme binds to enzyme N-terminus to maintain its zymogen form. Following secretion across a spore membrane, domain binds in trans to the C-terminus of another enzyme molecule thus facilitating first cleavage event of enzyme near the N-terminus which releases the enzyme from the forespore membrane
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant protein using His-tag
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)
-
expressed as His-tag fusion protein in Escherichia coli BL21(DE3) pLys
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3)
P17896
expression of wild-type and enzyme mutants in mutants strain BSL51 and R13
-
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
P26937
fusion protein with beta-galactosidase
P17896
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D137A
P26937
mutant shows no remaining sporulation activity
D137A
-
site-directed mutagenesis, mutant is completely impaired in pro-sigmaK processing
D137E
-
site-directed mutagenesis, mutant is completely impaired in pro-sigmaK processing
D137H
P26937
mutant shows no remaining sporulation activity
D137N
P26937
mutant shows highly reduced sporulation activity
D137N
-
site-directed mutagenesis, mutant is completely impaired in pro-sigmaK processing
D149N
-
impaired self-cleavage, no pro-sigmaK processing
D213L
P17896
phenotype indistinguishable from wild type, normal spore formation, slight accumulation of the 50 kDa species
D240L
P17896
phenotype indistinguishable from wild type, normal spore formation
D242L
P17896
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
P17896
phenotype indistinguishable from wild type, normal spore formation
D363L
P17896
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
P17896
phenotype indistinguishable from wild type, normal spore formation
E44A
P26937
mutant shows nearly no remaining sporulation activity
E44A
-
site-directed mutagenesis, no activity
E44D
P26937
mutant shows increased sporulation activity
E44D
-
site-directed mutagenesis, unaltered activity, similar to wild-type
E44Q
P26937
mutant shows highly reduced sporulation activity
E44Q
-
site-directed mutagenesis, no activity
G114A
-
self-cleavage and pro-sigmaK processing similar to wild-type enzyme
G114Q
-
impaired self-cleavage, delayed pro-sigmaK processing
G126A
-
self-cleavage and pro-sigmaK processing similar to wild-type enzyme
G126Q
-
self-cleavage and pro-sigmaK processing similar to wild-type enzyme
G138A
-
site-directed mutagenesis, slightly reduced activity
G139A
-
site-directed mutagenesis, slightly reduced activity
G144A
-
self-cleavage and pro-sigmaK processing similar to wild-type enzyme
G144A/N155D
-
self-cleavage and pro-sigmaK processing similar to wild-type enzyme
G144Q
-
self-cleavage and pro-sigmaK processing similar to wild-type enzyme
H236F
P17896
phenotype indistinguishable from null mutant, fails to trigger and sigmaK signaling and to form heat and lysozyme resistant spores
H236N
P17896
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
P17896
production of approximately 30% fewer spores than wild type, unable to germinate properly at 37°C
H43A
-
site-directed mutagenesis, no activity
H43F
P26937
mutant shows no remaining sporulation activity, no immunologically detectable enzyme protein
H43F
-
site-directed mutagenesis, extremely low enzyme expression, no activity
H47F
P26937
mutant shows no remaining sporulation activity
H47F
-
site-directed mutagenesis, no activity
I42P
P26937
mutant shows increased sporulation activity
K321A
P17896
phenotype indistinguishable from wild type, normal spore formation
N122A
-
site-directed mutagenesis, extremely low enzyme expression
N122D
-
site-directed mutagenesis, extremely low enzyme expression
N122Q
-
site-directed mutagenesis, unaltered activity, similar to wild-type
N129A
-
site-directed mutagenesis, slightly reduced activity
N155D
-
self-cleavage and pro-sigmaK processing similar to wild-type enzyme
N155Y
-
self-cleavage and pro-sigmaK processing similar to wild-type enzyme
N290I
P17896
production of approximately 30% fewer spores than wild type, unable to germinate properly at 37°C
P132A
-
site-directed mutagenesis, highly reduced enzyme activity
R185H
-
self-cleavage and pro-sigmaK processing similar to wild-type enzyme
R185K
-
self-cleavage and pro-sigmaK processing similar to wild-type enzyme
S378A
P17896
phenotype indistinguishable from null mutant, fails to trigger and sigmaK signaling and to form heat and lysozyme resistant spores
S378A
-
mutant with blocked self-cleavage
S378A
-
unable to process self cleavage, unable to trigger the activation of pro-sigmaK processing
S378K
P17896
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
S378A
Bacillus subtilis PV79
-
unable to process self cleavage, unable to trigger the activation of pro-sigmaK processing
-
D137N
-
mutant shows highly reduced sporulation activity
-
D213L
-
phenotype indistinguishable from wild type, normal spore formation, slight accumulation of the 50 kDa species
-
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
-
E44A
-
mutant shows nearly no remaining sporulation activity
-
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
-
H43F
-
mutant shows no remaining sporulation activity, no immunologically detectable enzyme protein
-
S378A
-
unable to process self cleavage, unable to trigger the activation of pro-sigmaK processing
-
K387A
P17896
phenotype indistinguishable from wild type, normal spore formation, slight accumulation of the 50 kDa species
additional information
P26937
comparison of effects of spoIVFB mutation with spoIVFB mutation on accumulation level of the enzymes in the recombinant strains, overview
additional information
-
N-terminal deletion of residues 1-35, 1-52, 1-62 or 1-74 and additional C-terminal deletion of up to 33 residues. Study on autoactivation process, which involves one trans cleavage by another enzyme protein and two cis cleavages
additional information
-
cellular localization of enzyme-GFP fusion protein
additional information
-
coexpression of enzyme and its substrate pro-sigmaK in Escherichia coli. Enzyme shows abundant and accurate cleavage of substrate. Coexpression of Bacillus subtilis protein BofA in this system leads to formation of a complex of enzyme and BofA and marked inhibition of pro-sigmaK processing. Inhibition may occur by providing H57 of BofA as metal ligand to the catalytic center of enzyme
T228A
-
can signal processing of pro-sigmaK but is unable to complete its non-signalling function
additional information
Bacillus subtilis PV79
-
cellular localization of enzyme-GFP fusion protein
-
I42P
-
mutant shows increased sporulation activity
-
additional information
-
cellular localization of enzyme-GFP fusion protein; comparison of effects of spoIVFB mutation with spoIVFB mutation on accumulation level of the enzymes in the recombinant strains, overview
-