Information on EC 3.4.24.B23 - stage IV sporulation protein FB

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The expected taxonomic range for this enzyme is: Bacillus subtilis

EC NUMBER
COMMENTARY hide
3.4.24.B23
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
stage IV sporulation protein FB
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
implicated in the coupling of mother cell to forespore gene expression. Required for spore formation. Processes the pro-sigma K factor
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PV79
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
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before sporulation, the transmembrane metalloprotease SpoIVFB is held inactive by two other integral-membrane proteins, SpoIVFA and BofA, with SpoIVFA playing an essential role in the complex formation, regulation, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pro-sigmaK + H2O
sigmaK + peptide
show the reaction diagram
pro-sigmaK + H2O
sigmaK + sigmaK propeptide
show the reaction diagram
pro-sigmaK S20G + H2O
sigmaK S20G + sigmaK propeptide
show the reaction diagram
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the substrate mutant is cleaved by the SpoIVFB protein with an extra transmembrane segment, but not by its mutant E44Q
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?
additional information
?
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regulation of SpoIVFB activity is achieved by a proteolytic cascade involving serine proteases, which are used as S1P protease in other S2P cascades. SpoIVB and CtpB are not involved in Site-1 cleavage of substrate but are required to relieve the inhibition of SpoIVFB by SpoIVFA and BofA
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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
pro-sigmaK + H2O
sigmaK + peptide
show the reaction diagram
pro-sigmaK + H2O
sigmaK + sigmaK propeptide
show the reaction diagram
additional information
?
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regulation of SpoIVFB activity is achieved by a proteolytic cascade involving serine proteases, which are used as S1P protease in other S2P cascades. SpoIVB and CtpB are not involved in Site-1 cleavage of substrate but are required to relieve the inhibition of SpoIVFB by SpoIVFA and BofA
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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required
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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required, the enzyme is a metalloprotease
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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BofA
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SpoIVFA
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additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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SpoIVFB activity requires ATP, which binds to the C-terminal cystathionine-beta-synthase domain of SpoIVFB. ATP probably regulates substrate access to the active site and renders cleavage sensitive to the cellular energy level
additional information
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incorporation of SpoIVFB into preformed liposomes stimulates its ability to cleave pro-sigmaK
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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early engulfment processes, discrete foci at the septum and very faint signal in the mother cell cytoplasmic membrane
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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SpoIVFB is unique among S2P family members in that it does not contain PDZ domain
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as GFP fusion protein
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expressed in Escherichia coli BL21(DE3) cells
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expression of functional SpoIVFB protein with an extra transmembrane segment attached to the N-terminus in Escherichia coli, the modification results in 100fold increased expression rate and facilitated purification
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E44C
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inactive
E44Q
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site-directed mutagenesis of SpoIVFB protein with an extra transmembrane segment , the mutant is inactive with substrate mutant pro-sigmaK S20G in contrast to the wild-type enzyme
E44Q/E282C
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inactive
additional information
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construction of SpoIVFB protein with an extra transmembrane segment attached to the N-terminus for increased expression rate and facilitated purification, overview. Deletion of 10 residues from the C-terminal end of SpoIVFB nearly eliminates cleavage of coexpressed pro-sigmaK in recombinant Escherichia coli