3.4.24.B23: stage IV sporulation protein FB
This is an abbreviated version!
For detailed information about stage IV sporulation protein FB, go to the full flat file.
Reaction
implicated in the coupling of mother cell to forespore gene expression. Required for spore formation. Processes the pro-sigma K factor =
Synonyms
More, pro-sigmaK protease, SPOIVFB, SpoIVFB protein
ECTree
3.4.24.B23 stage IV sporulation protein FBAdvanced search results
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General Information on EC 3.4.24.B23 - stage IV sporulation protein FB
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
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
physiological function
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SpoIVFB is a metalloprotease site-2 protease, S2P, that is involved in regulated intramembrane proteolysis, a conserved mechanism regulating signal transduction across the membrane by recruiting membrane-bound proteases to cleave membrane-spanning regulatory proteins, overview. It is involved in activation of the crucial membrane-associated transcription factors sigmaK during sporulation
physiological function
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SpoIVFB protein cleaves membrane-tethered Pro-sigmaK, releasing sigmaK to direct transcription of genes necessary for spore formation
physiological function
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the enzyme cleaves pro-sigmaK during Bacillus subtilis sporulation between Ser20 and Tyr21
physiological function
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the enzyme regulates Bacillus subtilis endospore formation by cleaving pro-sigmaK and releasing the active sigma factor from a membrane
physiological function
an inactive variant of SpoIVFB forms a stable complex with substrate Pro-sigmaK. Both the Pro(1-20) and sigmaK(21-126) parts contribute to the interaction, but only the sigmaK part is needed to form a stable complex. The last 10 residues of SpoIVFB are required. the complex has a 4:2 SpoIVFB:Pro-sigmaK(1-126) stoichiometry
physiological function
interaction of SpoIVFB with its substrate pro-sigmaK depends on particular residues in the interdomain linker of SpoIVFB. The linker plus either the N-terminal membrane domain or the C-terminal cystathione-beta-synthase domain of SpoIVFB is sufficient for the interaction but not for cleavage of pro-sigmaK
physiological function
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an inactive variant of SpoIVFB forms a stable complex with substrate Pro-sigmaK. Both the Pro(1-20) and sigmaK(21-126) parts contribute to the interaction, but only the sigmaK part is needed to form a stable complex. The last 10 residues of SpoIVFB are required. the complex has a 4:2 SpoIVFB:Pro-sigmaK(1-126) stoichiometry
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physiological function
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interaction of SpoIVFB with its substrate pro-sigmaK depends on particular residues in the interdomain linker of SpoIVFB. The linker plus either the N-terminal membrane domain or the C-terminal cystathione-beta-synthase domain of SpoIVFB is sufficient for the interaction but not for cleavage of pro-sigmaK
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