| IED ID | IndEnz0005000257 |
| Enzyme Type ID | lipase000257 |
| Protein Name |
Sensor histidine kinase LnrJ EC 2.7.13.3 |
| Gene Name | lnrJ linJ yfiJ BSU08290 |
| 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 | MKALFFTRMFTLMVSCLMYLSIVKEDNWFGYVFIAAGAAMYAANHVLLTKETNAIWFCLIDIAIGFSFGFIFPGTGLFIIMLCPVAVAFFLRGFPKRTAWSVLCLSSILFLTVLIRTYAMFGNEFVIDHLTSMTFVVFCGVVGKLIRKLLDAQDTAKQQFQELTESHLALSAAHQELHLYAKQVEELTAIYERNRMAREIHDTVGHKMTALLVQLQLLREWQKRDSQKADETVGVCETLAREALDDVRLSVRTLQTENDPSLIESLKQLTEDFCKNAGVTTEFAVSGDPAIIPLSLHPTLIRTVQEALTNAKRHGGAAACSIQLACTTDSISLVIKDDGKGNPEAALGFGLLNMKKRAAEHGGMIRFESERDQGFTVNAEFSLANKKWSFGPVQQKESLS |
| Enzyme Length | 400 |
| Uniprot Accession Number | P94438 |
| 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; Evidence={ECO:0000250|UniProtKB:P13799}; |
| DNA Binding | |
| EC Number | 2.7.13.3 |
| Enzyme Function | FUNCTION: Required for resistance to linearmycins, a family of antibiotic-specialized metabolites produced by some streptomycetes (PubMed:26647299, PubMed:28461449). Member of the two-component regulatory system LnrJ/LnrK, which induces expression of the LnrLMN ABC transporter in response to linearmycins and other polyenes (PubMed:11717295, PubMed:26647299, PubMed:28461449). Acts as a specific sensor for linearmycin, either directly through binding or indirectly through membrane perturbation. Probably activates LnrK by phosphorylation (PubMed:28461449). May also promote biofilm formation (PubMed:28461449). {ECO:0000269|PubMed:11717295, ECO:0000269|PubMed:26647299, ECO:0000269|PubMed:28461449}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Modified residue (1); Mutagenesis (1); Topological domain (6); Transmembrane (5) |
| Keywords | ATP-binding;Cell membrane;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Reference proteome;Transferase;Transmembrane;Transmembrane helix;Two-component regulatory system |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. |
| Modified Residue | MOD_RES 201; /note=Phosphohistidine; by autocatalysis; /evidence=ECO:0000250|UniProtKB:P13799 |
| Post Translational Modification | PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P13799}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 44,543 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |