| IED ID | IndEnz0002014324 |
| Enzyme Type ID | protease014324 |
| Protein Name |
Periplasmic pH-dependent serine endoprotease DegQ EC 3.4.21.107 Protease Do |
| Gene Name | degQ hhoA b3234 JW3203 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MKKQTQLLSALALSVGLTLSASFQAVASIPGQVADQAPLPSLAPMLEKVLPAVVSVRVEGTASQGQKIPEEFKKFFGDDLPDQPAQPFEGLGSGVIINASKGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIVSALGRSGLNLEGLENFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGFAIPSNMARTLAQQLIDFGEIKRGLLGIKGTEMSADIAKAFNLDVQRGAFVSEVLPGSGSAKAGVKAGDIITSLNGKPLNSFAELRSRIATTEPGTKVKLGLLRNGKPLEVEVTLDTSTSSSASAEMITPALEGATLSDGQLKDGGKGIKIDEVVKGSPAAQAGLQKDDVIIGVNRDRVNSIAEMRKVLAAKPAIIALQIVRGNESIYLLMR |
| Enzyme Length | 455 |
| Uniprot Accession Number | P39099 |
| Absorption | |
| Active Site | ACT_SITE 109; /note=Charge relay system; /evidence=ECO:0000269|PubMed:21685389; ACT_SITE 139; /note=Charge relay system; /evidence=ECO:0000269|PubMed:21685389; ACT_SITE 214; /note=Charge relay system; /evidence=ECO:0000269|PubMed:21685389 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP). {ECO:0000269|PubMed:8576051}. |
| Binding Site | BINDING 59; /note=Substrate; /evidence=ECO:0000250; BINDING 109; /note=Substrate; /evidence=ECO:0000250; BINDING 139; /note=Substrate; /evidence=ECO:0000250; BINDING 212; /note=Substrate; via amide nitrogen; /evidence=ECO:0000269|PubMed:21685389 |
| 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; |
| DNA Binding | |
| EC Number | 3.4.21.107 |
| Enzyme Function | FUNCTION: DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP. {ECO:0000269|PubMed:8576051, ECO:0000269|PubMed:8830688}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. The degradation is efficient at pH values between 4.5 and 6. {ECO:0000269|PubMed:21685389}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (17); Binding site (4); Chain (1); Domain (2); Helix (9); Mutagenesis (3); Region (3); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Direct protein sequencing;Hydrolase;Periplasm;Protease;Reference proteome;Repeat;Serine protease;Signal;Stress response |
| Interact With | Itself; P0A910 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8576051}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000269|PubMed:8576051 |
| Structure 3D | Electron microscopy (4); X-ray crystallography (2) |
| Cross Reference PDB | 3STI; 3STJ; 4A8A; 4A8B; 4A8C; 4A9G; |
| Mapped Pubmed ID | 15690043; 16606699; 22245966; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,205 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.107; |