| IED ID | IndEnz0002014321 |
| Enzyme Type ID | protease014321 |
| Protein Name |
Periplasmic serine endoprotease DegP EC 3.4.21.107 Heat shock protein DegP Protease Do |
| Gene Name | degP htrA ptd b0161 JW0157 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MKKTTLALSALALSLGLALSPLSATAAETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ |
| Enzyme Length | 474 |
| Uniprot Accession Number | P0C0V0 |
| Absorption | |
| Active Site | ACT_SITE 131; /note=Charge relay system; /evidence=ECO:0000269|PubMed:20581825; ACT_SITE 161; /note=Charge relay system; /evidence=ECO:0000269|PubMed:20581825; ACT_SITE 236; /note=Charge relay system; /evidence=ECO:0000269|PubMed:20581825 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP). {ECO:0000269|PubMed:2180903}. |
| Binding Site | BINDING 58; /note=Substrate; BINDING 131; /note=Substrate; BINDING 161; /note=Substrate |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.; EC=3.4.21.107; Evidence={ECO:0000269|PubMed:8830688}; |
| DNA Binding | |
| EC Number | 3.4.21.107 |
| Enzyme Function | FUNCTION: DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures (PubMed:10319814). Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions (PubMed:16303867). DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids (PubMed:8830688). Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins (PubMed:8830688). Its proteolytic activity is essential for the survival of cells at elevated temperatures (PubMed:7557477). It can degrade IciA, Ada, casein, globin and PapA. DegP shares specificity with DegQ (PubMed:8830688). DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP). {ECO:0000269|PubMed:10319814, ECO:0000269|PubMed:12730160, ECO:0000269|PubMed:16303867, ECO:0000269|PubMed:18496527, ECO:0000269|PubMed:18505836, ECO:0000269|PubMed:2180903, ECO:0000269|PubMed:7557477, ECO:0000269|PubMed:8830688}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is around 55 degrees Celsius. In the range from 37 to 55 degrees Celsius, the proteolytic activity rapidly increases with temperature. {ECO:0000269|PubMed:7744744}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (28); Binding site (3); Chain (1); Disulfide bond (1); Domain (2); Helix (10); Mutagenesis (8); Region (3); Sequence conflict (7); Signal peptide (1); Turn (6) |
| Keywords | 3D-structure;Cell inner membrane;Cell membrane;Direct protein sequencing;Disulfide bond;Hydrolase;Membrane;Protease;Reference proteome;Repeat;Serine protease;Signal;Stress response |
| Interact With | Itself; P0A910; P06996; P02666; P00698 |
| Induction | INDUCTION: By heat shock (PubMed:3057437). Transcriptionally up-regulated by sigma-E factor and the Cpx two-component signal transduction pathway (PubMed:7883164, PubMed:9351822). {ECO:0000269|PubMed:3057437, ECO:0000269|PubMed:7883164, ECO:0000269|PubMed:9351822}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:9083020}; Peripheral membrane protein {ECO:0000269|PubMed:9083020}; Cytoplasmic side {ECO:0000269|PubMed:9083020}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence="ECO:0000269|PubMed:2180903, ECO:0000269|PubMed:9600841" |
| Structure 3D | Electron microscopy (2); X-ray crystallography (11) |
| Cross Reference PDB | 1KY9; 2ZLE; 3CS0; 3MH4; 3MH5; 3MH6; 3MH7; 3OTP; 3OU0; 4A8D; 6JJK; 6JJL; 6JJO; |
| Mapped Pubmed ID | 15690043; 16606699; 22245966; 24373465; 25525882; 33005001; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,354 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.107; |