3.4.21.116: SpoIVB peptidase
This is an abbreviated version!
For detailed information about SpoIVB peptidase, go to the full flat file.
Word Map on EC 3.4.21.116
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3.4.21.116
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forespore
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pro-sigmak
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sigmak
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checkpoint
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bofa
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spoivfa
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metalloprotease
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intercompartmental
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ctpb
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membrane-embedded
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intramembrane
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cell-cell
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engulfment
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autoproteolysis
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zymogen
- 3.4.21.116
- forespore
- pro-sigmak
- sigmak
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checkpoint
- bofa
- spoivfa
- metalloprotease
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intercompartmental
- ctpb
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membrane-embedded
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intramembrane
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cell-cell
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engulfment
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autoproteolysis
- zymogen
Reaction
N-terminal cleavage of the pro-form of the sporulation protein sigmaK =
Synonyms
M50.002, S55.001, SpoIVB, SpoIVB serine peptidase, SpolVFB, sporulation protein SpolVFB, stage IV sporulation protein FB
ECTree
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Natural Substrates Products
Natural Substrates Products on EC 3.4.21.116 - SpoIVB peptidase
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REACTION DIAGRAM
pro-sigmaK
sigmaK + ?
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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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?
CtpB + H2O
?
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cleavage is not required to activate CtpB protease activity
-
-
?
CtpB + H2O
?
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cleavage is not required to activate CtpB protease activity
-
-
?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
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processing of prosigmaK, which is a protein involved in sporulation
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?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
processing of prosigmaK, which is a protein involved in sporulation
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?
pro-sigmaK + H2O
sigmaK + 20 amino acid peptide
processing of prosigmaK, which is a protein involved in sporulation
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?
?
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protein located in the forespore membrane, cleavage of the extracellular domain, involved in the regulation of sigmaK processing
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-
?
SpoIIQ + H2O
?
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protein located in the forespore membrane, cleavage of the extracellular domain, involved in the regulation of sigmaK processing
-
-
?
SpoIIQ + H2O
?
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protein located in the forespore membrane, cleavage of the extracellular domain, involved in the regulation of sigmaK processing
-
-
?
cleaved SpoIVFA + extracellular domain peptide of SpoIVFA
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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
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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
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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
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
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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
-
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
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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
-
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
-
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
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
-
-
?
cleaved SpoIVFA + extracellular domain peptides of SpoIVFA
-
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 peptides of SpoIVFA
-
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
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-
?
?
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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
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?
additional information
?
-
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enzyme is a critical component of the sigmaK regulatory checkpoint during spore formation, PDZ domain can interact with BofC
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?
additional information
?
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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
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?
additional information
?
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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
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-
?
additional information
?
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self cleavage into at least three distinct species of 46, 45, and 44 kDa
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-
?
additional information
?
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self cleavage into at least three distinct species of 46, 45, and 44 kDa
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-
?
additional information
?
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self cleavage into at least three distinct species of 46, 45, and 44 kDa
-
-
?