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
-
checkpoint
- bofa
- spoivfa
- metalloprotease
-
intercompartmental
- ctpb
-
membrane-embedded
-
intramembrane
-
cell-cell
-
engulfment
-
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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General Information
General Information on EC 3.4.21.116 - SpoIVB peptidase
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physiological function
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a stable association between the membrane-embedded protease SpoIVFB and its substrate requires SpoIVB signaling. The cytoplasmic cystathionine-beta-synthase domain of the SpoIVFB protease is not critical for this interaction or for pro-sigmaK processing. A model explains IVB-dependent cleavage of SpoIVFA on one side of the membrane triggers a conformational change in the membrane-embedded protease from a closed to an open state allowing pro-sigmaK access to the caged interior of the protease
physiological function
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a stable association between the membrane-embedded protease SpoIVFB and its substrate requires SpoIVB signaling. The cytoplasmic cystathionine-beta-synthase domain of the SpoIVFB protease is not critical for this interaction or for pro-sigmaK processing. A model explains IVB-dependent cleavage of SpoIVFA on one side of the membrane triggers a conformational change in the membrane-embedded protease from a closed to an open state allowing pro-sigmaK access to the caged interior of the protease
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