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Literature summary for 3.4.21.116 extracted from
- Evidence that SpoIVFB is a novel type of membrane metalloprotease governing intercompartmental communication during Bacillus subtilis sporulation (2000), J. Bacteriol., 182, 3305-3309.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| functional expression of wild-type, and expression of amino acid exchange mutants in the mutant strain BSL51, lacking spoIVFA and spoIVFB genes, and in the mutant OR745, lacking gene spoIVFB | Bacillus subtilis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D137A | mutant shows no remaining sporulation activity | Bacillus subtilis |
| D137H | mutant shows no remaining sporulation activity | Bacillus subtilis |
| D137N | mutant shows highly reduced sporulation activity | Bacillus subtilis |
| E44A | mutant shows nearly no remaining sporulation activity | Bacillus subtilis |
| E44D | mutant shows increased sporulation activity | Bacillus subtilis |
| E44Q | mutant shows highly reduced sporulation activity | Bacillus subtilis |
| H43F | mutant shows no remaining sporulation activity, no immunologically detectable enzyme protein | Bacillus subtilis |
| H47F | mutant shows no remaining sporulation activity | Bacillus subtilis |
| I42P | mutant shows increased sporulation activity | Bacillus subtilis |
| additional information | comparison of effects of spoIVFB mutation with spoIVFB mutation on accumulation level of the enzymes in the recombinant strains, overview | Bacillus subtilis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | belongs to the family of putative membrane metalloproteases | Bacillus subtilis | 16020 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pro-sigmaK + H2O | Bacillus subtilis | processing of prosigmaK, which is a protein involved in sporulation | sigmaK + 20 amino acid peptide | - |
? |  |
| pro-sigmaK + H2O | Bacillus subtilis PY79 | processing of prosigmaK, which is a protein involved in sporulation | sigmaK + 20 amino acid peptide | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | P26937 | - |
- |
| Bacillus subtilis PY79 | P26937 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| self-cleaves Val52-/-Asn53, Ala62-/-Phe63 and Val74-/-Thr75 at the N-terminus of SpoIVB | enzyme contains conserved metalloprotease sequence motif HEXXH | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pro-sigmaK + H2O | processing of prosigmaK, which is a protein involved in sporulation | Bacillus subtilis | sigmaK + 20 amino acid peptide | - |
? | |
| pro-sigmaK + H2O | processing of prosigmaK, which is a protein involved in sporulation | Bacillus subtilis PY79 | sigmaK + 20 amino acid peptide | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| M50.002 | Merops-ID | Bacillus subtilis |
| SpolVFB | - |
Bacillus subtilis |
| stage IV sporulation protein FB | - |
Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
in vivo assay at | Bacillus subtilis |
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