| IED ID | IndEnz0002012861 |
| Enzyme Type ID | protease012861 |
| Protein Name |
Protease 3 EC 3.4.24.55 Pitrilysin Protease III Protease pi |
| Gene Name | ptrA ptr STY3133 t2903 |
| Organism | Salmonella typhi |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica (Salmonella choleraesuis) Salmonella enterica I Salmonella typhi |
| Enzyme Sequence | MPRSTWFKALLLLVALWGPAVQADIGWQPLQETIRKSDKDTRQYQAIRLDNDMVVLLVSDPQAVKSLSALVVPVVSLEDPEAHQGLAHYLEHMCLMGSKKYPQADSLAEYLKRHGGSHNASTAPYRTAFYLEVENDALPGAVDRLADAIAAPLLNKKYAERERNAVNAELTMARTRDGMRMAQVSAETINPAHPGSHFSGGNLETLSDKPGNPVQQALIAFHEKYYSSNLMKAVIYSNKPLPELASIAAATYGRVPNKQIKKPEITVPVITEAQKGIIIHYVPALPRKVLRVEFRIDNNSAQFRSKTDELVSYLIGNRSPGTLSDWLQKQGLVEGISADSDPIVNGNSGVFAISATLTDKGLANRDEVVAAIFSYLNTLREKGIDKRYFDELAHVLDLDFRYPSITRDMDYVEWLADTMIRVPVAHTLDAANIADRYDPAAIKNRLAMMTPQNARIWYISPQEPHNKIAYFVDAPYQVDKISEQTFKNWQQKAQGIALSLPELNPYIPDDFTLIKNDKNYVRPELIVDKADLRVVYAPSRYFASEPKADVSVVLRNPQAMDSARNQVLFALNDYLAGMALDQLSNQAAVGGISFSTNANNGLMVTANGYTQRLPQLFLALLEGYFSYDATEEQLAQAKSWYTQMMDSAEKGKAYEQAIMPVQMISQVPYFSRDERRALLPSITLKEVMAYRNALKTGARPEFLVIGNMSEAQATSLAQDVQKQLAANGSAWCRNKDVVVEKKQSVIFEKAGSSTDSALAAVFVPVGYDEYVSAAYSAMLGQIVQPWFYNQLRTEEQLGYAVFAFPMSVGRQWGMGFLLQSNDKQPSYLWQRYQAFFPDAEAKLRAMKPEEFAQIQQAIITQMRQAPQTLGEEASRLSKDFDRGNMRFDSRDKIIAQIKLLTPQKLADFFHQAVVEPQGMAILSQIAGSQNGKAEYVHPTGWKVWDNVSALQQTLPLMSEKNE |
| Enzyme Length | 962 |
| Uniprot Accession Number | Q8Z418 |
| Absorption | |
| Active Site | ACT_SITE 91; /note=Proton acceptor; /evidence=ECO:0000250 |
| 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; |
| 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. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Signal peptide (1) |
| Keywords | Hydrolase;Magnesium;Metal-binding;Metalloprotease;Periplasm;Protease;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 107,524 |
| Kinetics | |
| Metal Binding | METAL 88; /note=Zinc; /evidence=ECO:0000250; METAL 92; /note=Zinc; /evidence=ECO:0000250; METAL 169; /note=Zinc; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |