Detail Information for IndEnz0005000120
IED ID IndEnz0005000120
Enzyme Type ID lipase000120
Protein Name Transcriptional regulatory protein LnrK
Gene Name lnrK linK yfiK BSU08300
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 MIKIIITDDQDIVREGLASLLQLREELDVIATARNGQEAFEKAKELEPDIVLMDIRMPVSNGVEGTKLITSSLPSVKVLMLTTFKDSALIAEALEEGASGYLLKDMSADTIVKAVMTVHSGGMVLPPELTAQMLNEWKREKQLKGINEIEKPNELLDLTEREIEVLAELGYGLNNKEIAEKLYITEGTVKNHVSNIISKLAVRDRTQAAIYSVRYGVSVF
Enzyme Length 220
Uniprot Accession Number P94439
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding DNA_BIND 175..194; /note=H-T-H motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU00411
EC Number
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). Probably binds to the promoter region of the lnrLMN operon and directly regulates its expression (Probable). May also promote biofilm formation (PubMed:28461449). {ECO:0000269|PubMed:11717295, ECO:0000269|PubMed:26647299, ECO:0000269|PubMed:28461449, ECO:0000305|PubMed:28461449}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); DNA binding (1); Domain (2); Modified residue (1); Mutagenesis (1)
Keywords Activator;Cytoplasm;DNA-binding;Phosphoprotein;Reference proteome;Transcription;Transcription regulation;Two-component regulatory system
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
Modified Residue MOD_RES 54; /note=4-aspartylphosphate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00169
Post Translational Modification PTM: Phosphorylated by LnrJ. {ECO:0000305|PubMed:28461449}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 24,371
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda