| IED ID | IndEnz0002007602 |
| Enzyme Type ID | protease007602 |
| Protein Name |
Protease 3 EC 3.4.24.55 Pitrilysin Protease III Protease pi |
| Gene Name | ptrA ptr b2821 JW2789 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MPRSTWFKALLLLVALWAPLSQAETGWQPIQETIRKSDKDNRQYQAIRLDNGMVVLLVSDPQAVKSLSALVVPVGSLEDPEAYQGLAHYLEHMSLMGSKKYPQADSLAEYLKMHGGSHNASTAPYRTAFYLEVENDALPGAVDRLADAIAEPLLDKKYAERERNAVNAELTMARTRDGMRMAQVSAETINPAHPGSKFSGGNLETLSDKPGNPVQQALKDFHEKYYSANLMKAVIYSNKPLPELAKMAADTFGRVPNKESKKPEITVPVVTDAQKGIIIHYVPALPRKVLRVEFRIDNNSAKFRSKTDELITYLIGNRSPGTLSDWLQKQGLVEGISANSDPIVNGNSGVLAISASLTDKGLANRDQVVAAIFSYLNLLREKGIDKQYFDELANVLDIDFRYPSITRDMDYVEWLADTMIRVPVEHTLDAVNIADRYDAKAVKERLAMMTPQNARIWYISPKEPHNKTAYFVDAPYQVDKISAQTFADWQKKAADIALSLPELNPYIPDDFSLIKSEKKYDHPELIVDESNLRVVYAPSRYFASEPKADVSLILRNPKAMDSARNQVMFALNDYLAGLALDQLSNQASVGGISFSTNANNGLMVNANGYTQRLPQLFQALLEGYFSYTATEDQLEQAKSWYNQMMDSAEKGKAFEQAIMPAQMLSQVPYFSRDERRKILPSITLKEVLAYRDALKSGARPEFMVIGNMTEAQATTLARDVQKQLGADGSEWCRNKDVVVDKKQSVIFEKAGNSTDSALAAVFVPTGYDEYTSSAYSSLLGQIVQPWFYNQLRTEEQLGYAVFAFPMSVGRQWGMGFLLQSNDKQPSFLWERYKAFFPTAEAKLRAMKPDEFAQIQQAVITQMLQAPQTLGEEASKLSKDFDRGNMRFDSRDKIVAQIKLLTPQKLADFFHQAVVEPQGMAILSQISGSQNGKAEYVHPEGWKVWENVSALQQTMPLMSEKNE |
| Enzyme Length | 962 |
| Uniprot Accession Number | P05458 |
| Absorption | |
| Active Site | ACT_SITE 91; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:1570301, ECO:0000269|PubMed:8099278" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of 16-Tyr-|-Leu-17 and 25-Phe-|-Tyr-26 bonds of oxidized insulin B chain. Also acts on other substrates of Mw less than 7 kDa such as insulin and glucagon.; EC=3.4.24.55; Evidence={ECO:0000255|PROSITE-ProRule:PRU10096}; |
| DNA Binding | |
| EC Number | 3.4.24.55 |
| Enzyme Function | FUNCTION: Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (29); Chain (1); Helix (42); Metal binding (3); Mutagenesis (6); Sequence conflict (1); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Hydrolase;Magnesium;Metal-binding;Metalloprotease;Periplasm;Protease;Reference proteome;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1Q2L; |
| Mapped Pubmed ID | 15502359; 16606699; 7674955; 7674956; |
| Motif | |
| Gene Encoded By | |
| Mass | 107,708 |
| Kinetics | |
| Metal Binding | METAL 88; /note="Zinc"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:1570301"; METAL 92; /note="Zinc"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:1570301"; METAL 169; /note="Zinc" |
| Rhea ID | |
| Cross Reference Brenda |