IED ID | IndEnz0005000121 |
Enzyme Type ID | lipase000121 |
Protein Name |
Linearmycin resistance ATP-binding protein LnrL EC 7.6.2.- |
Gene Name | lnrL bifL yfiL BSU08310 |
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 | MLQAENIKKAYGKKTIVKGISFSLKKGESFGLLGPNGAGKSTTISMISGLVPHDSGNITVGGYVIGKETAKAKQKIGIVPQEIALYPTLTAHENLMFWGKMYGLTHGEAKKRAAEVLEYVGLTERAKDKIETFSGGMKRRINIGAALMHKPELLIMDEPTVGIDPQSRNHILETVKQLNETGMTVIYTSHYMEEVEFLCDRIGIIDQGEMIAIGTKTDLCSRLGGDTIIQLTVSGINEAFLVAIRSLAHVNDVTVHELELKIDISAAHHEKVVTSLLAEATAHHINLLSLQVQEPNLERLFLNLTGRTLRD |
Enzyme Length | 311 |
Uniprot Accession Number | P94440 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 7.6.2.- |
Enzyme Function | FUNCTION: Required for resistance to linearmycins, a family of antibiotic-specialized metabolites produced by some streptomycetes (PubMed:26647299, PubMed:28461449). Part of the ABC transporter complex LnrLMN that probably facilitates linearmycin removal from the membrane. Responsible for energy coupling to the transport system (PubMed:28461449). Also mediates KinC-dependent biofilm morphology (PubMed:28461449). {ECO:0000269|PubMed:26647299, ECO:0000269|PubMed:28461449}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | NP_BIND 34..41; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00434 |
Features | Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (1) |
Keywords | ATP-binding;Nucleotide-binding;Reference proteome;Translocase;Transport |
Interact With | |
Induction | INDUCTION: Induced in response to linearmycins and other polyenes via the two-component regulatory system LnrJ/LnrK. {ECO:0000269|PubMed:28461449}. |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 34,050 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |