| IED ID | IndEnz0002007043 |
| Enzyme Type ID | protease007043 |
| Protein Name |
Metalloprotease LoiP EC 3.4.24.- |
| Gene Name | loiP yggG b2936 JW2903 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MKIRALLVAMSVATVLTGCQNMDSNGLLSSGAEAFQAYSLSDAQVKTLSDQACQEMDSKATIAPANSEYAKRLTTIANALGNNINGQPVNYKVYMAKDVNAFAMANGCIRVYSGLMDMMTDNEVEAVIGHEMGHVALGHVKKGMQVALGTNAVRVAAASAGGIVGSLSQSQLGNLGEKLVNSQFSQRQEAEADDYSYDLLRQRGISPAGLATSFEKLAKLEEGRQSSMFDDHPASAERAQHIRDRMSADGIK |
| Enzyme Length | 252 |
| Uniprot Accession Number | P25894 |
| Absorption | |
| Active Site | ACT_SITE 131; /evidence=ECO:0000255 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. {ECO:0000269|PubMed:1310091, ECO:0000269|PubMed:17651431, ECO:0000269|PubMed:17909889, ECO:0000269|PubMed:22491786}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (1); Erroneous initiation (2); Lipidation (2); Metal binding (3); Region (1); Signal peptide (1) |
| Keywords | Cell outer membrane;Disulfide bond;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Palmitate;Protease;Reference proteome;Signal;Stress response;Zinc |
| Interact With | P0A6D5 |
| Induction | INDUCTION: Induced by heat shock and low osmolarity. {ECO:0000269|PubMed:17651431, ECO:0000269|PubMed:17909889, ECO:0000269|PubMed:22491786}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:17909889, ECO:0000269|PubMed:22491786}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:17909889, ECO:0000269|PubMed:22491786}. Note=Proper membrane localization can depend on BepA. |
| Modified Residue | |
| Post Translational Modification | PTM: The intramolecular disulfide bond improves the stability and the activity of LoiP. It forms even in the absence of the oxido-reductase DsbA (PubMed:22491786). {ECO:0000269|PubMed:22491786}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255|PROSITE-ProRule:PRU00303 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15690043; 16606699; |
| Motif | |
| Gene Encoded By | |
| Mass | 26,842 |
| Kinetics | |
| Metal Binding | METAL 130; /note=Zinc; catalytic; /evidence=ECO:0000255; METAL 134; /note=Zinc; catalytic; /evidence=ECO:0000255; METAL 189; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |