| IED ID | IndEnz0002003649 |
| Enzyme Type ID | protease003649 |
| Protein Name |
Metallopeptidase AprA EC 3.4.24.- Heat-resistant peptidase |
| Gene Name | aprA |
| Organism | Pseudomonas panacis |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas panacis |
| Enzyme Sequence | MSKAKDKAIVSAAQASTAYSQIDSFSHLYDRGGNLTINGKPSYTVDQAATQLLRDGAAYRDFDGNGKIDLTYTFLTSASSSTMNKHGISGFSQFNAQQKAQAALAMQSWSDVANVTFTEKASGGDGHMTFGNYSSGQDGAAAFAYLPGTGAGYDGTSWYLTNNSYTPNKTPDLNNYGRQTLTHEIGHTLGLAHPGDYNAGEGAPTYNDATYGQDTRGYSLMSYWSESNTNQNFSKGGVEAYASGPLIDDIAAIQKLYGANYNTRAGDTTYGFNSNTGRDFLSATSNADKLVFSVWDGGGNDTLDFSGFTQNQKINLNEASFSDVGGLVGNVSIAKGVTIENAFGGAGNDLIIGNNAANVIKGGAGNDLIYGAGGADQLWGGAGNDTFVFGASSDSKPGAADKIFDFTSGSDKIDLSGITKGAGLTFVNAFTGHAGDAVLTYAAGTNLGTLAVDFSGHGVADFLVTTVGQAAVSDIVA |
| Enzyme Length | 477 |
| Uniprot Accession Number | A0A0C5CJR8 |
| Absorption | |
| Active Site | ACT_SITE 184; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Is completely inhibited by the metal cation chelators 1,10-phenanthroline and EDTA, but PMSF, pepstatin A and E-64 have no effect on activity. {ECO:0000269|Ref.1}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Peptidase able to cleave azocasein and the milk substrates beta-casein and Na-caseinate. Can withstand UHT processing of milk, and is able to spoil UHT milk over the storage period. {ECO:0000269|Ref.1}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. At higher temperatures, the activity decreases rapidly. Shows high enzyme activity with casein as a substrate under the storage conditions of UHT milk. Is highly thermostable. Withstands general ultra-high temperature (UHT) processing (138 degrees Celsius for 18 seconds) in skim milk, with 88% of the initial enzyme activity remaining after heating. The milk matrix has a protective effect on the enzyme activity during the thermal process. {ECO:0000269|Ref.1}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|Ref.1}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (43); Repeat (3); Signal peptide (1) |
| Keywords | Calcium;Hydrolase;Metal-binding;Metalloprotease;Protease;Repeat;Secreted;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,380 |
| Kinetics | |
| Metal Binding | METAL 183; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 187; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 193; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 264; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 266; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 268; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 296; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 298; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 299; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 301; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 301; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 338; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 340; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 345; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 347; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 349; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 354; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 356; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 358; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 362; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 363; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 364; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 365; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 367; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 367; /note=Calcium 5; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 371; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 372; /note=Calcium 6; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 373; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 374; /note=Calcium 6; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 376; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 376; /note=Calcium 6; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 380; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 381; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 382; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 383; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 385; /note=Calcium 5; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 385; /note=Calcium 7; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 394; /note=Calcium 6; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 401; /note=Calcium 6; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 411; /note=Calcium 7; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 453; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 455; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:Q03023; METAL 461; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:Q03023 |
| Rhea ID | |
| Cross Reference Brenda |