Detail Information for IndEnz0005000064
IED ID IndEnz0005000064
Enzyme Type ID lipase000064
Protein Name Response regulator protein PmrA
Gene Name pmrA PA4776
Organism Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Enzyme Sequence MRILLAEDDLLLGDGIRAGLRLEGDTVEWVTDGVAAENALVTDEFDLLVLDIGLPRRSGLDILRNLRHQGLLTPVLLLTARDKVADRVAGLDSGADDYLTKPFDLDELQARVRALTRRTTGRALPQLVHGELRLDPATHQVTLSGQAVELAPREYALLRLLLENSGKVLSRNQLEQSLYGWSGDVESNAIEVHVHHLRRKLGNQLIRTVRGIGYGIDQPAP
Enzyme Length 221
Uniprot Accession Number Q9HV32
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding DNA_BIND 124..218; /note=OmpR/PhoB-type; /evidence=ECO:0000255|PROSITE-ProRule:PRU01091
EC Number
Enzyme Function FUNCTION: Member of the two-component regulatory system PmrA/PmrB that plays a role in the regulation of resistance towards polymyxin B and cationic antimicrobial peptides in response to limiting concentrations of Mg(2+) (PubMed:14507375). Functions as a transcriptional activator by direct binding to a cis-acting sequence upstream of the target gene promoters including lipase lipA and pmrH promoters (PubMed:16707691, PubMed:29379484). Autoregulates also its own pmrAB operon under Mg(2+)-limiting conditions (PubMed:14507375, PubMed:16707691). {ECO:0000269|PubMed:14507375, ECO:0000269|PubMed:16707691, ECO:0000269|PubMed:29379484}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); DNA binding (1); Domain (1); Modified residue (1)
Keywords Cytoplasm;DNA-binding;Phosphoprotein;Reference proteome;Transcription;Transcription regulation;Two-component regulatory system
Interact With
Induction INDUCTION: By cationic antimicrobial peptides and by Mg(2+)-limiting conditions. {ECO:0000269|PubMed:14507375}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
Modified Residue MOD_RES 51; /note=4-aspartylphosphate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00169
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 24,394
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda