| IED ID | IndEnz0002006647 |
| Enzyme Type ID | protease006647 |
| Protein Name |
Sporulation kinase C EC 2.7.13.3 |
| Gene Name | kinC mskA ssb BSU14490 |
| 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 | MRKYQARIISIILAMIFIMFWDYLFYFIGKNPINWPVDIVYTAVTLVSVWMLAYYIDEKQQLVKKMKDNEWKYKQLSEEKNRIMDNLQEIVFQTNAKGEITYLNQAWASITGFSISECMGTMYNDYFIKEKHVADHINTQIQNKASSGMFTAKYVTKNGTIFWGEVHYKLYYDRDDQFTGSLGTMSDITERKEAEDELIEINERLARESQKLSITSELAAGIAHEVRNPLTSVSGFLQIMKTQYPDRKDYFDIIFSEIKRIDLVLSELLLLAKPQAITFKTHQLNEILKQVTTLLDTNAILSNIVIEKNFKETDGCMINGDENQLKQVFINIIKNGIEAMPKGGVVTISTAKTASHAVISVKDEGNGMPQEKLKQIGKPFYSTKEKGTGLGLPICLRILKEHDGELKIESEAGKGSVFQVVLPLKSDS |
| Enzyme Length | 428 |
| Uniprot Accession Number | P39764 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; |
| DNA Binding | |
| EC Number | 2.7.13.3 |
| Enzyme Function | FUNCTION: Phosphorylates the sporulation-regulatory protein Spo0A a transcription factor that also controls biofilm formation (Probable). Requires FloT and FloA for localization to DRMs and for activity (PubMed:20713508). {ECO:0000269|PubMed:20713508, ECO:0000305|PubMed:8002614}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (3); Modified residue (1); Transmembrane (2) |
| Keywords | ATP-binding;Cell membrane;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Reference proteome;Sporulation;Transferase;Transmembrane;Transmembrane helix;Two-component regulatory system |
| Interact With | |
| Induction | INDUCTION: Induced at the onset of sporulation, shuts off at T3. May be under the control of Spo0A. {ECO:0000269|PubMed:8002615}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:26297017, ECO:0000269|PubMed:27362352}; Multi-pass membrane protein. Membrane raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:26297017, ECO:0000269|PubMed:27362352}; Multi-pass membrane protein {ECO:0000255}. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion. Lost from DRM in the absence of farnesyl diphosphate phosphatase YisP or when cells are treated with YisP inhibitor zaragozic acid. Colocalizes with FloT in DRMs (PubMed:20713508, PubMed:26297017). Another study shows KinC foci are membrane assemblies of 85-110 nm, but found no evidence of colocalization of these foci with FloA or FloT (PubMed:27362352). {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:26297017, ECO:0000269|PubMed:27362352}. |
| Modified Residue | MOD_RES 224; /note=Phosphohistidine; by autocatalysis; /evidence=ECO:0000255|PROSITE-ProRule:PRU00107 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 21630458; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,846 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 2.7.13.3; |