| IED ID | IndEnz0002001868 |
| Enzyme Type ID | protease001868 |
| Protein Name |
Regulator of sigma-E protease RseP EC 3.4.24.- S2P endopeptidase Site-2 protease RseP S2P protease RseP Site-2-type intramembrane protease |
| Gene Name | rseP ecfE yaeL b0176 JW0171 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MLSFLWDLASFIVALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDKLGTEYVIALIPLGGYVKMLDERAEPVVPELRHHAFNNKSVGQRAAIIAAGPVANFIFAIFAYWLVFIIGVPGVRPVVGEIAANSIAAEAQIAPGTELKAVDGIETPDWDAVRLQLVDKIGDESTTITVAPFGSDQRRDVKLDLRHWAFEPDKEDPVSSLGIRPRGPQIEPVLENVQPNSAASKAGLQAGDRIVKVDGQPLTQWVTFVMLVRDNPGKSLALEIERQGSPLSLTLIPESKPGNGKAIGFVGIEPKVIPLPDEYKVVRQYGPFNAIVEATDKTWQLMKLTVSMLGKLITGDVKLNNLSGPISIAKGAGMTAELGVVYYLPFLALISVNLGIINLFPLPVLDGGHLLFLAIEKIKGGPVSERVQDFCYRIGSILLVLLMGLALFNDFSRL |
| Enzyme Length | 450 |
| Uniprot Accession Number | P0AEH1 |
| Absorption | |
| Active Site | ACT_SITE 23; /evidence=ECO:0000305 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by Zn(2+) chelator 1,10-phenanthroline. {ECO:0000269|PubMed:21810987}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA, residue 'Val-148' of RseA may be required for this. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA. Can also cleave sequences in transmembrane regions of other proteins (such as LacY) as well as liberated signal peptides of beta-lactamase, OmpF, LivK, SecM, PhoA, LivJ, OmpC, Lpp and TorA, probably within the membrane. {ECO:0000269|PubMed:12183368, ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:15496982, ECO:0000269|PubMed:18268014, ECO:0000269|PubMed:18945679, ECO:0000269|PubMed:21810987}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (14); Chain (1); Domain (2); Helix (4); Metal binding (2); Mutagenesis (28); Topological domain (3); Transmembrane (4); Turn (3) |
| Keywords | 3D-structure;Cell inner membrane;Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | INDUCTION: Part of the sigma-E regulon. Also has a primary sigma-70 factor promoter. {ECO:0000269|PubMed:11274153}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11689431, ECO:0000269|PubMed:11750129, ECO:0000269|PubMed:11867724, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:11689431, ECO:0000269|PubMed:11750129, ECO:0000269|PubMed:11867724, ECO:0000269|PubMed:15919996}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 2ZPL; 2ZPM; 3ID1; 3ID2; 3ID3; 3ID4; |
| Mapped Pubmed ID | 15690043; 17179147; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,071 |
| Kinetics | |
| Metal Binding | METAL 22; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 26; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |