| IED ID | IndEnz0002001502 |
| Enzyme Type ID | protease001502 |
| Protein Name |
Stage IV sporulation protein A EC 3.6.1.- Coat morphogenetic protein SpoIVA |
| Gene Name | spoIVA spoVP BSU22800 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MEKVDIFKDIAERTGGDIYLGVVGAVRTGKSTFIKKFMELVVLPNISNEADRARAQDELPQSAAGKTIMTTEPKFVPNQAMSVHVSDGLDVNIRLVDCVGYTVPGAKGYEDENGPRMINTPWYEEPIPFHEAAEIGTRKVIQEHSTIGVVITTDGTIGDIARSDYIEAEERVIEELKEVGKPFIMVINSVRPYHPETEAMRQDLSEKYDIPVLAMSVESMRESDVLSVLREALYEFPVLEVNVNLPSWVMVLKENHWLRESYQESVKETVKDIKRLRDVDRVVGQFSEFEFIESAGLAGIELGQGVAEIDLYAPDHLYDQILKEVVGVEIRGRDHLLELMQDFAHAKTEYDQVSDALKMVKQTGYGIAAPALADMSLDEPEIIRQGSRFGVRLKAVAPSIHMIKVDVESEFAPIIGTEKQSEELVRYLMQDFEDDPLSIWNSDIFGRSLSSIVREGIQAKLSLMPENARYKLKETLERIINEGSGGLIAIIL |
| Enzyme Length | 492 |
| Uniprot Accession Number | P35149 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:18691972, ECO:0000269|PubMed:23267091}; |
| DNA Binding | |
| EC Number | 3.6.1.- |
| Enzyme Function | FUNCTION: ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM. {ECO:0000269|PubMed:1729246, ECO:0000269|PubMed:17427285, ECO:0000269|PubMed:18691972, ECO:0000269|PubMed:23267091, ECO:0000269|PubMed:8299942}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 24..31; /note=ATP; /evidence=ECO:0000305 |
| Features | Chain (1); Motif (1); Mutagenesis (24); Nucleotide binding (1) |
| Keywords | ATP-binding;Cytoplasm;Direct protein sequencing;Hydrolase;Nucleotide-binding;Reference proteome;Sporulation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Uniformly distributed on the membrane around the forespore, lying close to or on its outer surface. Expression only necessary in the mother cell chamber of the sporangium for the formation of a mature spore. According to PubMed:8299942, not a coat protein of the mature spore, is only transiently associated with the assembling coat. According to PubMed:9922240, present as a component of the fully mature spore. Proper localization requires the expression of a gene spoVM which is under the control of the mother cell transcription factor sigma E. {ECO:0000269|PubMed:1729247, ECO:0000269|PubMed:17427285, ECO:0000269|PubMed:18691972, ECO:0000269|PubMed:19775244, ECO:0000269|PubMed:23267091, ECO:0000269|PubMed:8299942, ECO:0000269|PubMed:8936302, ECO:0000269|PubMed:9922240}. |
| Modified Residue | |
| Post Translational Modification | PTM: Seems to be cleaved by the YabG protease. {ECO:0000269|PubMed:11040425}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 24..31; /note=Walker A motif; involved in ATP-binding and hydrolysis |
| Gene Encoded By | |
| Mass | 55,175 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=412 uM for ATP {ECO:0000269|PubMed:18691972, ECO:0000269|PubMed:23267091}; Note=The turnover rate is 2.7 pmol/min/pmol of SpoIVA at Vmax (PubMed:18691972). The turnover rate is 1.0 pmol/min/pmol of SpoIVA at Vmax (PubMed:23267091). {ECO:0000269|PubMed:18691972, ECO:0000269|PubMed:23267091}; |
| Metal Binding | |
| Rhea ID | RHEA:13065 |
| Cross Reference Brenda |