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 |
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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 |
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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 |
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Gene Encoded By |
|
Mass |
26,312 |
Kinetics |
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Metal Binding |
|
Rhea ID |
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Cross Reference Brenda |
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