| IED ID | IndEnz0002007295 |
| Enzyme Type ID | protease007295 |
| Protein Name |
Pseudomonalisin EC 3.4.21.100 Pepstatin-insensitive carboxyl proteinase Pseudomonapepsin |
| Gene Name | pcp |
| Organism | Pseudomonas sp. (strain 101) (Achromobacter parvulus T1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Proteobacteria incertae sedis unclassified pseudomonads Pseudomonas sp. (strain 101) (Achromobacter parvulus T1) |
| Enzyme Sequence | MKSSAAKQTVLCLNRYAVVALPLAIASFAAFGASPASTLWAPTDTKAFVTPAQVEARSAAPLLELAAGETAHIVVSLKLRDEAQLKQLAQAVNQPGNAQFGKFLKRRQFLSQFAPTEAQVQAVVAHLRKNGFVNIHVVPNRLLISADGSAGAVKAAFNTPLVRYQLNGKAGYANTAPAQVPQDLGEIVGSVLGLQNVTRAHPMLKVGERSAAKTLAAGTAKGHNPTEFPTIYDASSAPTAANTTVGIITIGGVSQTLQDLQQFTSANGLASVNTQTIQTGSSNGDYSDDQQGQGEWDLDSQSIVGSAGGAVQQLLFYMADQSASGNTGLTQAFNQAVSDNVAKVINVSLGWCEADANADGTLQAEDRIFATAAAQGQTFSVSSGDEGVYECNNRGYPDGSTYSVSWPASSPNVIAVGGTTLYTTSAGAYSNETVWNEGLDSNGKLWATGGGYSVYESKPSWQSVVSGTPGRRLLPDISFDAAQGTGALIYNYGQLQQIGGTSLASPIFVGLWARLQSANSNSLGFPAASFYSAISSTPSLVHDVKSGNNGYGGYGYNAGTGWDYPTGWGSLDIAKLSAYIRSNGFGH |
| Enzyme Length | 587 |
| Uniprot Accession Number | P42790 |
| Absorption | |
| Active Site | ACT_SITE 295; /note=Charge relay system; /evidence=ECO:0000269|PubMed:10488127; ACT_SITE 299; /note=Charge relay system; /evidence=ECO:0000269|PubMed:10488127; ACT_SITE 502; /note=Charge relay system; /evidence=ECO:0000269|PubMed:10488127 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the B chain of insulin at 13-Glu-|-Ala-14, 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 and angiotensin I at 4-Tyr-|-Ile-5. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-|-Phe(NO(2))-Arg-Leu.; EC=3.4.21.100; |
| DNA Binding | |
| EC Number | 3.4.21.100 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (17); Chain (1); Disulfide bond (1); Domain (1); Helix (13); Metal binding (5); Propeptide (2); Region (1); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Periplasm;Protease;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm. |
| Modified Residue | |
| Post Translational Modification | PTM: Autocatalytically processed. |
| Signal Peptide | SIGNAL 1..?; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (9) |
| Cross Reference PDB | 1GA1; 1GA4; 1GA6; 1NLU; 6M8W; 6M8Y; 6M9C; 6M9D; 6M9F; |
| Mapped Pubmed ID | 11173470; |
| Motif | |
| Gene Encoded By | |
| Mass | 61,073 |
| Kinetics | |
| Metal Binding | METAL 543; /note=Calcium; METAL 544; /note=Calcium; via carbonyl oxygen; METAL 559; /note=Calcium; via carbonyl oxygen; METAL 561; /note=Calcium; via carbonyl oxygen; METAL 563; /note=Calcium |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.100; |