Any feedback?
Literature summary extracted from
- New insights into S2P signaling cascades: regulation, variation and conservation (2010), Protein Sci., 19, 2015-2030.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.B23 | BofA | inhibits SpoIVFB probably by supplying a fourth zinc ligand. SpoIVFB inhibition is relieved by two serine proteases SpoIVB and CtpB | Bacillus subtilis | |
| 3.4.24.B23 | additional information | 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 | Bacillus subtilis | |
| 3.4.24.B23 | SpoIVFA | SpoIVFB inhibition is relieved by two serine proteases SpoIVB and CtpB | Bacillus subtilis | |
| 3.4.24.85 | additional information | SpoIVFB is held inactive by two other integral-membrane proteins, SpoIVFA and BofA | Bacillus subtilis |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.24.B23 | membrane | - |
Bacillus subtilis | 16020 | - |
| 3.4.24.85 | cytoplasmic membrane | - |
Escherichia coli | - |
- |
| 3.4.24.85 | cytoplasmic membrane | - |
Mycobacterium tuberculosis | - |
- |
| 3.4.24.85 | cytoplasmic membrane | - |
Caulobacter vibrioides | - |
- |
| 3.4.24.85 | cytoplasmic membrane | - |
Cryptococcus neoformans | - |
- |
| 3.4.24.85 | cytoplasmic membrane | - |
Streptococcus uberis | - |
- |
| 3.4.24.85 | Golgi apparatus | - |
Bacillus subtilis | 5794 | - |
| 3.4.24.85 | Golgi apparatus | - |
Homo sapiens | 5794 | - |
| 3.4.24.85 | Golgi apparatus | - |
Enterococcus faecalis | 5794 | - |
| 3.4.24.85 | membrane | - |
Pseudomonas aeruginosa | 16020 | - |
| 3.4.24.85 | membrane | - |
Bordetella bronchiseptica | 16020 | - |
| 3.4.24.85 | membrane | periplasmic | Mycobacterium tuberculosis | 16020 | - |
| 3.4.24.85 | membrane | periplasmic | Streptococcus uberis | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.85 | Zn2+ | a zinc metalloprotease | Bacillus subtilis |  |
| 3.4.24.85 | Zn2+ | a zinc metalloprotease | Escherichia coli | |
| 3.4.24.85 | Zn2+ | a zinc metalloprotease | Homo sapiens | |
| 3.4.24.85 | Zn2+ | a zinc metalloprotease | Pseudomonas aeruginosa | |
| 3.4.24.85 | Zn2+ | a zinc metalloprotease | Bordetella bronchiseptica | |
| 3.4.24.85 | Zn2+ | a zinc metalloprotease | Enterococcus faecalis | |
| 3.4.24.85 | Zn2+ | a zinc metalloprotease | Mycobacterium tuberculosis | |
| 3.4.24.85 | Zn2+ | a zinc metalloprotease | Caulobacter vibrioides | |
| 3.4.24.85 | Zn2+ | a zinc metalloprotease | Cryptococcus neoformans | |
| 3.4.24.85 | Zn2+ | a zinc metalloprotease | Streptococcus uberis | |
| 3.4.24.85 | Zn2+ | a zinc metalloprotease | Methanocaldococcus jannaschii | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.B23 | additional information | Bacillus subtilis | 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 | ? | - |
? | |
| 3.4.24.B23 | pro-sigmaK + H2O | Bacillus subtilis | maturation and activation of sigmaK by proteolytic removal of an N-terminal extension of 20 amino acids. Pro-sigmaK is associated with the outer forespore membrane with its N-terminal transmembrane segment, amino acids 1 to 27. Proteolytic cleavage by SpoIVFB releases the C-terminal sigmaK into the mother cell for directing transcription of genes involved in spore cortex and coat synthesis | sigmaK + sigmaK propeptide | - |
? | |
| 3.4.24.85 | ATF6 protein + H2O | Homo sapiens | - |
? | - |
? | |
| 3.4.24.85 | cAD1 protein + H2O | Enterococcus faecalis | - |
? | - |
? | |
| 3.4.24.85 | cCF10 protein + H2O | Enterococcus faecalis | - |
? | - |
? | |
| 3.4.24.85 | cPD1 protein + H2O | Enterococcus faecalis | - |
? | - |
? | |
| 3.4.24.85 | CREBH protein + H2O | Homo sapiens | - |
? | - |
? | |
| 3.4.24.85 | FtsL protein + H2O | Bacillus subtilis | - |
? | - |
? | |
| 3.4.24.85 | HurR protein + H2O | Bordetella bronchiseptica | - |
? | - |
? | |
| 3.4.24.85 | iAD1 protein + H2O | Enterococcus faecalis | - |
? | - |
? | |
| 3.4.24.85 | iCF10 protein + H2O | Enterococcus faecalis | - |
? | - |
? | |
| 3.4.24.85 | MtuA protein + H2O | Streptococcus uberis | - |
? | - |
? | |
| 3.4.24.85 | MucA protein + H2O | Pseudomonas aeruginosa | - |
? | - |
? | |
| 3.4.24.85 | OASIS protein + H2O | Homo sapiens | - |
? | - |
? | |
| 3.4.24.85 | PBP3 protein + H2O | Mycobacterium tuberculosis | - |
? | - |
? | |
| 3.4.24.85 | PodJ protein + H2O | Caulobacter vibrioides | - |
? | - |
? | |
| 3.4.24.85 | pro-deltaK protein + H2O | Bacillus subtilis | - |
deltaK protein + N-terminal fragment of 20 amino acids of pro-deltaK protein | - |
? | |
| 3.4.24.85 | RseA protein + H2O | Escherichia coli | - |
? | - |
? | |
| 3.4.24.85 | RsiW protein + H2O | Bacillus subtilis | - |
? | - |
? | |
| 3.4.24.85 | Sre1 protein + H2O | Cryptococcus neoformans | - |
? | - |
? | |
| 3.4.24.85 | sterol regulatory element binding protein + H2O | Homo sapiens | - |
? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.24.B23 | Bacillus subtilis | - |
- |
- |
| 3.4.24.85 | Bacillus subtilis | - |
- |
- |
| 3.4.24.85 | Bordetella bronchiseptica | - |
- |
- |
| 3.4.24.85 | Caulobacter vibrioides | - |
- |
- |
| 3.4.24.85 | Cryptococcus neoformans | - |
- |
- |
| 3.4.24.85 | Enterococcus faecalis | - |
- |
- |
| 3.4.24.85 | Escherichia coli | - |
- |
- |
| 3.4.24.85 | Homo sapiens | - |
- |
- |
| 3.4.24.85 | Methanocaldococcus jannaschii | - |
- |
- |
| 3.4.24.85 | Mycobacterium tuberculosis | - |
- |
- |
| 3.4.24.85 | Pseudomonas aeruginosa | - |
- |
- |
| 3.4.24.85 | Streptococcus uberis | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.B23 | additional information | 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 | Bacillus subtilis | ? | - |
? | |
| 3.4.24.B23 | pro-sigmaK + H2O | maturation and activation of sigmaK by proteolytic removal of an N-terminal extension of 20 amino acids. Pro-sigmaK is associated with the outer forespore membrane with its N-terminal transmembrane segment, amino acids 1 to 27. Proteolytic cleavage by SpoIVFB releases the C-terminal sigmaK into the mother cell for directing transcription of genes involved in spore cortex and coat synthesis | Bacillus subtilis | sigmaK + sigmaK propeptide | - |
? | |
| 3.4.24.B23 | pro-sigmaK + H2O | proteolytic removal of an N-terminal extension of 20 amino acids | Bacillus subtilis | sigmaK + sigmaK propeptide | - |
? | |
| 3.4.24.85 | ATF6 protein + H2O | - |
Homo sapiens | ? | - |
? | |
| 3.4.24.85 | cAD1 protein + H2O | - |
Enterococcus faecalis | ? | - |
? | |
| 3.4.24.85 | cCF10 protein + H2O | - |
Enterococcus faecalis | ? | - |
? | |
| 3.4.24.85 | cPD1 protein + H2O | - |
Enterococcus faecalis | ? | - |
? | |
| 3.4.24.85 | CREBH protein + H2O | - |
Homo sapiens | ? | - |
? | |
| 3.4.24.85 | FtsL protein + H2O | - |
Bacillus subtilis | ? | - |
? | |
| 3.4.24.85 | HurR protein + H2O | - |
Bordetella bronchiseptica | ? | - |
? | |
| 3.4.24.85 | iAD1 protein + H2O | - |
Enterococcus faecalis | ? | - |
? | |
| 3.4.24.85 | iCF10 protein + H2O | - |
Enterococcus faecalis | ? | - |
? | |
| 3.4.24.85 | MtuA protein + H2O | - |
Streptococcus uberis | ? | - |
? | |
| 3.4.24.85 | MucA protein + H2O | - |
Pseudomonas aeruginosa | ? | - |
? | |
| 3.4.24.85 | OASIS protein + H2O | - |
Homo sapiens | ? | - |
? | |
| 3.4.24.85 | PBP3 protein + H2O | - |
Mycobacterium tuberculosis | ? | - |
? | |
| 3.4.24.85 | PodJ protein + H2O | - |
Caulobacter vibrioides | ? | - |
? | |
| 3.4.24.85 | pro-deltaK protein + H2O | - |
Bacillus subtilis | deltaK protein + N-terminal fragment of 20 amino acids of pro-deltaK protein | - |
? | |
| 3.4.24.85 | RseA protein + H2O | - |
Escherichia coli | ? | - |
? | |
| 3.4.24.85 | RsiW protein + H2O | - |
Bacillus subtilis | ? | - |
? | |
| 3.4.24.85 | Sre1 protein + H2O | - |
Cryptococcus neoformans | ? | - |
? | |
| 3.4.24.85 | sterol regulatory element binding protein + H2O | - |
Homo sapiens | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.24.B23 | More | SpoIVFB is unique among S2P family members in that it does not contain PDZ domain | Bacillus subtilis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.24.B23 | More | the enzyme belongs to the S2P family of metalloproteases, but SpoIVFB is unique among S2P family members in that it does not contain PDZ domain | Bacillus subtilis |
| 3.4.24.B23 | SPOIVFB | - |
Bacillus subtilis |
| 3.4.24.85 | EcfE | - |
Escherichia coli |
| 3.4.24.85 | Eep | - |
Enterococcus faecalis |
| 3.4.24.85 | Eep | - |
Streptococcus uberis |
| 3.4.24.85 | HurP | - |
Bordetella bronchiseptica |
| 3.4.24.85 | MmpA | - |
Caulobacter vibrioides |
| 3.4.24.85 | MucP | - |
Pseudomonas aeruginosa |
| 3.4.24.85 | RasP | - |
Bacillus subtilis |
| 3.4.24.85 | RseP | - |
Escherichia coli |
| 3.4.24.85 | Rv2869c | - |
Mycobacterium tuberculosis |
| 3.4.24.85 | S2P | - |
Bacillus subtilis |
| 3.4.24.85 | S2P | - |
Escherichia coli |
| 3.4.24.85 | S2P | - |
Homo sapiens |
| 3.4.24.85 | S2P | - |
Pseudomonas aeruginosa |
| 3.4.24.85 | S2P | - |
Bordetella bronchiseptica |
| 3.4.24.85 | S2P | - |
Enterococcus faecalis |
| 3.4.24.85 | S2P | - |
Mycobacterium tuberculosis |
| 3.4.24.85 | S2P | - |
Caulobacter vibrioides |
| 3.4.24.85 | S2P | - |
Cryptococcus neoformans |
| 3.4.24.85 | S2P | - |
Streptococcus uberis |
| 3.4.24.85 | S2P | - |
Methanocaldococcus jannaschii |
| 3.4.24.85 | site-2 protease | - |
Bacillus subtilis |
| 3.4.24.85 | site-2 protease | - |
Escherichia coli |
| 3.4.24.85 | site-2 protease | - |
Homo sapiens |
| 3.4.24.85 | site-2 protease | - |
Pseudomonas aeruginosa |
| 3.4.24.85 | site-2 protease | - |
Bordetella bronchiseptica |
| 3.4.24.85 | site-2 protease | - |
Enterococcus faecalis |
| 3.4.24.85 | site-2 protease | - |
Mycobacterium tuberculosis |
| 3.4.24.85 | site-2 protease | - |
Caulobacter vibrioides |
| 3.4.24.85 | site-2 protease | - |
Cryptococcus neoformans |
| 3.4.24.85 | site-2 protease | - |
Streptococcus uberis |
| 3.4.24.85 | site-2 protease | - |
Methanocaldococcus jannaschii |
| 3.4.24.85 | SPOIVFB | - |
Bacillus subtilis |
| 3.4.24.85 | Stp1 | - |
Cryptococcus neoformans |
| 3.4.24.85 | YaeL | - |
Escherichia coli |
| 3.4.24.85 | YluC | - |
Bacillus subtilis |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.24.B23 | additional information | 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 | Bacillus subtilis |
| 3.4.24.B23 | physiological function | 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 | Bacillus subtilis |
| 3.4.24.85 | physiological function | HurP is essential for heme-dependent induction of bhuR and downstream genes | Bordetella bronchiseptica |
| 3.4.24.85 | physiological function | the enzyme is involved in activation of the crucial membrane-associated transcription factors deltaK during sporulation | Bacillus subtilis |
| 3.4.24.85 | physiological function | the enzyme is involved in the feedback regulation of sterol and fatty acid synthesis and uptake by controlling the activity of transcription factors, sterol regulatory element binding proteins. Through the S2P cascade, the cholesterol feedback pathway in humans is stringently regulated | Homo sapiens |
| 3.4.24.85 | physiological function | the enzyme is involved in the production of pheromone cAD1, cPD1, and cCF10, and inhibitor peptide iAD1 and iCF10.The enzyme processes the sex pheromone and inhibitor precursors as they pass through the cell membrane | Enterococcus faecalis |
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