| IED ID | IndEnz0002004786 |
| Enzyme Type ID | protease004786 |
| Protein Name |
Serine endoprotease DegS EC 3.4.21.107 Site-1 protease DegS S1P protease DegS Site-1-type intramembrane protease |
| Gene Name | degS hhoB htrH b3235 JW3204 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MFVKLLRSVAIGLIVGAILLVAMPSLRSLNPLSTPQFDSTDETPASYNLAVRRAAPAVVNVYNRGLNTNSHNQLEIRTLGSGVIMDQRGYIITNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATGGLPTIPINARRVPHIGDVVLAIGNPYNLGQTITQGIISATGRIGLNPTGRQNFLQTDASINHGNSGGALVNSLGELMGINTLSFDKSNDGETPEGIGFAIPFQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQGIVVNEVSPDGPAANAGIQVNDLIISVDNKPAISALETMDQVAEIRPGSVIPVVVMRDDKQLTLQVTIQEYPATN |
| Enzyme Length | 355 |
| Uniprot Accession Number | P0AEE3 |
| Absorption | |
| Active Site | ACT_SITE 96; /note="Charge relay system"; /evidence="ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286"; ACT_SITE 126; /note="Charge relay system"; /evidence="ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286"; ACT_SITE 201; /note="Charge relay system"; /evidence="ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286" |
| Activity Regulation | ACTIVITY REGULATION: Allosterically activated by the C-terminus of exposed OMP peptides (consensus Tyr-X-Phe-COOH); cleavage only occurs in the presence of peptides. Inhibited when RseB is bound to RseA. {ECO:0000269|PubMed:12679035, ECO:0000269|PubMed:17360428, ECO:0000269|PubMed:17938245, ECO:0000269|PubMed:19836340, ECO:0000269|PubMed:20739286}. |
| Binding Site | BINDING 184; /note=Substrate; BINDING 351; /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; |
| DNA Binding | |
| EC Number | 3.4.21.107 |
| Enzyme Function | FUNCTION: A site-1 protease (S1P) that cleaves the peptide bond between 'Val-148' and 'Ser-149' in RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porins (OMP) and then initiates RseA (anti sigma-E factor) degradation by cleaving its periplasmic domain, making it a substrate for subsequent cleavage by RseP. This cascade ultimately leads to the sigma-E-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly. Required for basal and stress-induced degradation of RseA. {ECO:0000269|PubMed:10500101, ECO:0000269|PubMed:11442831, ECO:0000269|PubMed:12183368, ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:12679035, ECO:0000269|PubMed:17360428, ECO:0000269|PubMed:17938245, ECO:0000269|PubMed:18945679, ECO:0000269|PubMed:19695325, ECO:0000269|PubMed:19706448}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (23); Binding site (2); Chain (1); Domain (1); Helix (8); Mutagenesis (14); Region (1); Sequence conflict (2); Topological domain (2); Transmembrane (1); Turn (5) |
| Keywords | 3D-structure;Cell inner membrane;Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;Serine protease;Transmembrane;Transmembrane helix |
| Interact With | Itself; P0AFX7 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:11442831}; Single-pass membrane protein {ECO:0000305|PubMed:11442831}. Note=It is unclear how this protein is anchored to the inner membrane, programs predict a signal sequence, but replacing the N-terminal 26 residues with a known signal sequence gives a protein unable to fully complement a disruption mutant. {ECO:0000269|PubMed:11442831}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (29) |
| Cross Reference PDB | 1SOT; 1SOZ; 1TE0; 1VCW; 2QF0; 2QF3; 2QGR; 2R3U; 2R3Y; 2RCE; 3B8J; 3GCN; 3GCO; 3GDS; 3GDU; 3GDV; 3LGI; 3LGT; 3LGU; 3LGV; 3LGW; 3LGY; 3LH1; 3LH3; 4RQY; 4RQZ; 4RR0; 4RR1; 6EW9; |
| Mapped Pubmed ID | 12730160; 16606699; 19103920; 25703375; 29658704; |
| Motif | |
| Gene Encoded By | |
| Mass | 37,581 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33 uM for RseA-YQF {ECO:0000269|PubMed:17981123, ECO:0000269|PubMed:19836340}; Vmax=0.6 umol/sec/mg enzyme {ECO:0000269|PubMed:17981123, ECO:0000269|PubMed:19836340}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.107; |