| IED ID | IndEnz0002004611 |
| Enzyme Type ID | protease004611 |
| Protein Name |
Periplasmic serine endoprotease DegP EC 3.4.21.107 Heat shock protein DegP Protease Do |
| Gene Name | degP htrA ptd STM0209 |
| Organism | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica (Salmonella choleraesuis) Salmonella enterica I Salmonella typhimurium Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Enzyme Sequence | MKKTTLAMSALALSLGLALSPLSATAAETSSSAMTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQDGSPFQNSPFCQGGGNGGNGGQQQKFMALGSGVIIDAAKGYVVTNNHVVDNASVIKVQLSDGRKFDAKVVGKDPRSDIALIQIQNPKNLTAIKLADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNVENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVMPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKISLGLLREGKAITVNLELQQSSQSQVDSSTIFSGIEGAEMSNKGQDKGVVVSSVKANSPAAQIGLKKGDVIIGANQQPVKNIAELRKILDSKPSVLALNIQRGDSSIYLLMQ |
| Enzyme Length | 475 |
| Uniprot Accession Number | P26982 |
| Absorption | |
| Active Site | ACT_SITE 132; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P0C0V0; ACT_SITE 162; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P0C0V0; ACT_SITE 237; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P0C0V0 |
| Activity Regulation | |
| Binding Site | BINDING 59; /note=Substrate; /evidence=ECO:0000250; BINDING 132; /note=Substrate; /evidence=ECO:0000250; BINDING 162; /note=Substrate; /evidence=ECO:0000250 |
| 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: DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolytic activity is essential for the survival of cells at elevated temperatures. It can degrade IciA, ada, casein, globin and PapA. DegP shares specificity with DegQ. DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP) (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (3); Chain (1); Disulfide bond (1); Domain (2); Region (3); Signal peptide (1) |
| Keywords | Cell inner membrane;Cell membrane;Disulfide bond;Hydrolase;Membrane;Protease;Reference proteome;Repeat;Serine protease;Signal;Stress response |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19246758; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,315 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.107; |