| IED ID | IndEnz0002013055 |
| Enzyme Type ID | protease013055 |
| Protein Name |
Sensory/regulatory protein RpfC EC 2.7.13.3 |
| Gene Name | rpfC XC_2333 |
| Organism | Xanthomonas campestris pv. campestris (strain 8004) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Xanthomonas Xanthomonas campestris Xanthomonas campestris pv. campestris Xanthomonas campestris pv. campestris (strain 8004) |
| Enzyme Sequence | MKSPLPWLKRRLSGRADSEHAQNLIRIIITTLFISYLGWRYQHTHGDTLMATWLILVGELLVSLGLMVAILLRPQVSHTRRLIGMLLDYTCTGAIMAIQGEPASPLYAVCMWVTIGNGLRYGSNYLRAATAMGSLCFLGAILISPYWKANPYLSWGLLLGLIAVPLYFDSLLRAMTRAVREARHANQAKSRFLANMSHEFRTPLNGLSGMTEVLATTRLDAEQKECLNTIQASARSLLSLVEEVLDISAIEAGKIRIDRRDFSLREMIGSVNLILQPQARGRRLEYGTQVADDVPDLLKGDTAHLRQVLLNLVGNAVKFTEHGHVLLRVTRVSGSAEDAVRLRFDVEDTGIGVPMDMRPRLFEAFEQADVGLSRRYEGTGLGTTIAKGLVEAMGGSIGFKENQPSGSVFWFELPMAIGEPLKSSTVRVPTGALVDAPEELESSNIIAFSNPFLRHRARVRSMRMLVADDHEANRMVLQRLLEKAGHKVLCVNGAEQVLDAMAEEDYDAVIVDLHMPGMNGLDMLKQLRVMQASGMRYTPVVVLSADVTPEAIRACEQAGARAFLAKPVLAAKLLDTLADLAVSTRQLATPATTVQVATSFEGVLDSSVLDELAALGMGEEFERQFVRQCLDDAQNCVGDIERDGTCSDWEQLRESAHALRGVASNLGLAQVASSGGELMRMADWQLQAEWRLRLSTLREQLKAGKDALDARVQGVKDGECSPRSNE |
| Enzyme Length | 726 |
| Uniprot Accession Number | P0C0F7 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Binding of DSF to the sensor region causes allosteric change, which facilitates RpfC autophosphorylation. {ECO:0000269|PubMed:28369120}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000305|PubMed:28369120}; |
| DNA Binding | |
| EC Number | 2.7.13.3 |
| Enzyme Function | FUNCTION: Hybrid sensor kinase that regulates diverse biological functions through two distinct molecular mechanisms (PubMed:16940295). At low cell density, the extracellular concentration of the diffusible signaling factor (DSF) is below a threshold, and unphosphorylated RpfC is involved in the negative regulation of DSF synthesis, via direct interaction with the DSF synthase RpfF. Interaction prevents synthesis of DSF, which remains at a basal level. This activity does not involve the phosphorelay mechanism and is not dependent on RpfG (PubMed:11123673, PubMed:16940295). Is also member of the two-component regulatory system RpfG/RpfC, which is involved in the perception and response to DSF, which is essential for cell-cell signaling (PubMed:11123673, PubMed:12960398). At high cell density, the level of extracellular DSF increases and binding of DSF to the sensor region of RpfC causes autophosphorylation of RpfC, which results in the release of RpfF and the activation of RpfG via a four-step phosphorelay (PubMed:16940295, PubMed:28369120). Activation of RpfG leads to the positive regulation of biofilm dispersal and the production of virulence factors (PubMed:12960398). {ECO:0000269|PubMed:11123673, ECO:0000269|PubMed:12960398, ECO:0000269|PubMed:16940295, ECO:0000269|PubMed:28369120}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (3); Modified residue (3); Mutagenesis (14); Region (1); Sequence conflict (2); Topological domain (6); Transmembrane (5) |
| Keywords | ATP-binding;Cell inner membrane;Cell membrane;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Transcription;Transcription regulation;Transferase;Transmembrane;Transmembrane helix;Two-component regulatory system;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:28369120}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes at the cell poles. {ECO:0000269|PubMed:20231439}. |
| Modified Residue | MOD_RES 198; /note=Phosphohistidine; by autocatalysis; /evidence=ECO:0000255|PROSITE-ProRule:PRU00107; MOD_RES 512; /note=4-aspartylphosphate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00169; MOD_RES 657; /note=Phosphohistidine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00110 |
| Post Translational Modification | PTM: Autophosphorylated (PubMed:28369120). Activation may require a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain (Probable). {ECO:0000269|PubMed:28369120, ECO:0000305}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 79,806 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |