Detail Information for IndEnz0002016115
IED ID IndEnz0002016115
Enzyme Type ID protease016115
Protein Name Transcriptional regulatory protein CpxR
Gene Name cpxR yiiA b3912 JW3883
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MNKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSIDLLLLDVMMPKKNGIDTLKALRQTHQTPVIMLTARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSHWSEQQQNNDNGSPTLEVDALVLNPGRQEASFDGQTLELTGTEFTLLYLLAQHLGQVVSREHLSQEVLGKRLTPFDRAIDMHISNLRRKLPDRKDGHPWFKTLRGRGYLMVSAS
Enzyme Length 232
Uniprot Accession Number P0AE88
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: The two-component system is activated by envelope stress such as overexpression of some (misfolded) periplasmic proteins (PubMed:7883164, PubMed:9351822). Activated by spheroplasting (which removes the periplasm) in an autoregulatory cpxA-cpxR-dependent fashion (PubMed:10972835). Cpx two-component system is activated at pH 8.0; in a degP deletion mutant activation is halved (PubMed:9473036, PubMed:16166523). The CpxA kinase activity is inhibited by periplasmic accessory protein CpxP; proteolysis of CpxP relieves inhibition (PubMed:16166523, PubMed:17259177, PubMed:25207645). {ECO:0000269|PubMed:10972835, ECO:0000269|PubMed:16166523, ECO:0000269|PubMed:7883164, ECO:0000269|PubMed:9351822, ECO:0000269|PubMed:9473036}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding DNA_BIND 131..230; /note=OmpR/PhoB-type; /evidence=ECO:0000255|PROSITE-ProRule:PRU01091
EC Number
Enzyme Function FUNCTION: Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA (PubMed:7883164, PubMed:9401031). Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation (PubMed:11830644). Induced upon cell surface binding, subsequently induces genes it controls (cpxP, dsbA and spy, degP is only partially induced) (PubMed:11830644). Binds and activates transcription from the degP promoter (PubMed:7883164); binding is enhanced by phosphorylation (PubMed:9401031). This system combats a variety of extracytoplasmic protein-mediated toxicities by increasing the transcription of the periplasmic protease, DegP in concert with sigma factor E (PubMed:7883164), as well as that of CpxP protein. Other downstream effectors may include SrkA (PubMed:23416055). {ECO:0000269|PubMed:11830644, ECO:0000269|PubMed:23416055, ECO:0000269|PubMed:7883164, ECO:0000269|PubMed:9401031}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (11); Chain (1); DNA binding (1); Domain (1); Helix (8); Modified residue (1); Turn (4)
Keywords 3D-structure;Activator;Cell adhesion;Cytoplasm;DNA-binding;Phosphoprotein;Reference proteome;Stress response;Transcription;Transcription regulation;Two-component regulatory system
Interact With P0AE82; P00861; P0AG86
Induction INDUCTION: Induced about 3-fold when stationary phase cells bind to hydrophobic surfaces; requires direct contact with hydrophobic surfaces for up-regulation of Cpx activity (PubMed:11830644). {ECO:0000269|PubMed:11830644}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
Modified Residue MOD_RES 51; /note=4-aspartylphosphate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00169
Post Translational Modification PTM: Phosphorylated by CpxA. {ECO:0000269|PubMed:17259177, ECO:0000269|PubMed:9401031, ECO:0000305|PubMed:7883164}.
Signal Peptide
Structure 3D X-ray crystallography (4)
Cross Reference PDB 4UHJ; 4UHK; 4UHS; 4UHT;
Mapped Pubmed ID 1482126; 15686558; 15690043; 16077119; 16487683; 16606699; 18631241; 2157156; 24561554; 28552574; 30086390; 7699720; 8098993; 9159398;
Motif
Gene Encoded By
Mass 26,312
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda