| IED ID | IndEnz0002007300 |
| Enzyme Type ID | protease007300 |
| Protein Name |
M-protease EC 3.4.21.- |
| Gene Name | aprE ABC0761 |
| Organism | Bacillus clausii (strain KSM-K16) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Alkalihalobacillus Alkalihalobacillus clausii (Bacillus clausii) Bacillus clausii (strain KSM-K16) |
| Enzyme Sequence | MKKPLGKIVASTALLISVAFSSSIASAAEEAKEKYLIGFNEQEAVSEFVEQIEANDDVAILSEEEEVEIELLHEFETIPVLSVELSPEDVDALELDPTISYIEEDAEVTTMAQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGNGHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGASGSGSVSSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGAGSISYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGVAALVKQKNPSWSNVQIRNHLKNTATGLGNTNLYGSGLVNAEAATR |
| Enzyme Length | 380 |
| Uniprot Accession Number | Q99405 |
| Absorption | |
| Active Site | ACT_SITE 143; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 173; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 326; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | ACTIVITY REGULATION: Activity is inhibited by phenylmethylsulfonyl fluoride and chymostatin. {ECO:0000269|PubMed:7632397}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Alkaline serine protease that cleaves various substrates, including N-succinyl-Ala-Ala-Pro-Phe-pNA, N-succinyl-Ala-Ala-Pro-MetpNA, oxidized insulin B chain, casein, hemoglobin and scleroproteins, such as keratin, alpha-keratin and elastin. {ECO:0000269|PubMed:7632397}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. CaC1(2) markedly shifts the optimum temperature to 70 degrees Celsius. {ECO:0000269|PubMed:7632397}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 12.3. {ECO:0000269|PubMed:7632397}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (12); Chain (1); Domain (2); Helix (9); Metal binding (10); Propeptide (1); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:7632397}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1MPT; 1WSD; |
| Mapped Pubmed ID | 9278275; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,881 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 mM for N-succinyl-Ala-Ala-Pro-Phe-pNA {ECO:0000269|PubMed:7632397}; KM=1.01 mM for N-succinyl-Ala-Ala-Pro-Met-pNA {ECO:0000269|PubMed:7632397}; |
| Metal Binding | METAL 113; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:15299321, ECO:0007744|PDB:1MPT, ECO:0007744|PDB:1WSD"; METAL 151; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:15299321, ECO:0007744|PDB:1MPT, ECO:0007744|PDB:1WSD"; METAL 184; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:15299321, ECO:0007744|PDB:1MPT, ECO:0007744|PDB:1WSD"; METAL 186; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:15299321, ECO:0007744|PDB:1WSD"; METAL 188; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:15299321, ECO:0007744|PDB:1MPT, ECO:0007744|PDB:1WSD"; METAL 190; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:15299321, ECO:0007744|PDB:1MPT, ECO:0007744|PDB:1WSD"; METAL 274; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:15299321, ECO:0007744|PDB:1MPT"; METAL 276; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:15299321, ECO:0007744|PDB:1MPT"; METAL 279; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:15299321, ECO:0007744|PDB:1MPT"; METAL 302; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:15299321, ECO:0007744|PDB:1MPT" |
| Rhea ID | |
| Cross Reference Brenda |