| IED ID | IndEnz0002018701 |
| Enzyme Type ID | protease018701 |
| Protein Name |
D-aminopeptidase EC 3.4.11.- |
| Gene Name | dppA dciAA BSU12920 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MKLYMSVDMEGISGLPDDTFVDSGKRNYERGRLIMTEEANYCIAEAFNSGCTEVLVNDSHSKMNNLMVEKLHPEADLISGDVKPFSMVEGLDDTFRGALFLGYHARASTPGVMSHSMIFGVRHFYINDRPVGELGLNAYVAGYYDVPVLMVAGDDRAAKEAEELIPNVTTAAVKQTISRSAVKCLSPAKAGRLLTEKTAFALQNKDKVKPLTPPDRPVLSIEFANYGQAEWANLMPGTEIKTGTTTVQFQAKDMLEAYQAMLVMTELAMRTSFC |
| Enzyme Length | 274 |
| Uniprot Accession Number | P26902 |
| Absorption | |
| Active Site | ACT_SITE 115; /note=Nucleophile |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Hydrolyzes N-terminal residues in D-amino acid containing peptides. Among the tested substrates, the highest activities are with D-Ala-D-Ala and D-Ala-Gly-Gly. The physiological role is not clear. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9-11.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (14); Chain (1); Helix (9); Metal binding (6); Sequence conflict (2); Turn (1) |
| Keywords | 3D-structure;Aminopeptidase;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Sporulation;Zinc |
| Interact With | |
| Induction | INDUCTION: Nutrient deficiency conditions, which also induce sporulation. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1HI9; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 30,159 |
| Kinetics | |
| Metal Binding | METAL 8; /note=Zinc 1; METAL 8; /note=Zinc 2; METAL 10; /note=Zinc 1; METAL 60; /note=Zinc 2; METAL 104; /note=Zinc 2; METAL 133; /note=Zinc 2 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.19; |