| IED ID | IndEnz0002003438 |
| Enzyme Type ID | protease003438 |
| Protein Name |
Signal transduction histidine-protein kinase ArlS EC 2.7.13.3 |
| Gene Name | arlS SAOUHSC_01419 |
| Organism | Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Enzyme Sequence | MTKRKLRNNWIIVTTMITFVTIFLFCLIIIFFLKDTLHNSELDDAERSSSDINNLFHSKPVKDISALDLNASLGNFQEIIIYDEHNNKLFETSNDNTVRVEPGYEHRYFDRVIKKRYKGIEYLIIKEPITTQDFKGYSLLIHSLENYDNIVKSLYIIALAFGVIATIITATISYVFSTQITKPLVSLSNKMIEIRRDGFQNKLQLNTNYEEIDNLANTFNEMMSQIEESFNQQRQFVEDASHELRTPLQIIQGHLNLIQRWGKKDPAVLEESLNISIEEMNRIIKLVEELLELTKGDVNDISSEAQTVHINDEIRSRIHSLKQLHPDYQFDTDLTSKNLEIKMKPHQFEQLFLIFIDNAIKYDVKNKKIKVKTRLKNKQKIIEITDHGIGIPEEDQDFIFDRFYRVDKSRSRSQGGNGLGLSIAQKIIQLNGGSIKIKSEINKGTTFKIIF |
| Enzyme Length | 451 |
| Uniprot Accession Number | Q9KJN3 |
| 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: Member of the two-component regulatory system ArlS/ArlR involved in the regulation of adhesion, autolysis, multidrug resistance and virulence. ArlS probably functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to ArlR. ArlS/ArlR affects expression of the multidrug resistance transporter norA and interacts with both Agr (virulence accessory gene regulator) (negatively) and SarA (staphylococcal accessory regulator) (positively) to modulate several virulence factor genes, including ssp (serine protease), spa (surface protein A) and hla (alpha-hemolysin). Could inhibit biofilm development by a mechanism independent of the presence of the poly-N-acetylglucosamine (PNAG). Also, Arl proteins are required for the efficient activity of DNA gyrase inhibitors and high osmolarity on spa expression. {ECO:0000269|PubMed:10633099, ECO:0000269|PubMed:10869073, ECO:0000269|PubMed:11454217, ECO:0000269|PubMed:15528666, ECO:0000269|PubMed:16030226}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (2); Modified residue (1); Transmembrane (2) |
| Keywords | ATP-binding;Cell membrane;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Reference proteome;Transferase;Transmembrane;Transmembrane helix;Two-component regulatory system;Virulence |
| Interact With | |
| Induction | INDUCTION: Activated by agr, SarA, SarV and MgrA. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. |
| Modified Residue | MOD_RES 242; /note=Phosphohistidine; by autocatalysis; /evidence=ECO:0000255|PROSITE-ProRule:PRU00107 |
| Post Translational Modification | PTM: Autophosphorylated. {ECO:0000305}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,400 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |