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 |
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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 |
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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 |
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Structure 3D |
|
Cross Reference PDB |
- |
Mapped Pubmed ID |
- |
Motif |
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Gene Encoded By |
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Mass |
24,371 |
Kinetics |
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Metal Binding |
|
Rhea ID |
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Cross Reference Brenda |
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