| IED ID | IndEnz0002004973 |
| Enzyme Type ID | protease004973 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase DacA CPase DD-carboxypeptidase DD-peptidase EC 3.4.16.4 Penicillin-binding protein 5 PBP-5 |
| Gene Name | dacA BSU00100 |
| 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 | MNIKKCKQLLMSLVVLTLAVTCLAPMSKAKAASDPIDINASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLLEAIDQGKVKWDQTYTPDDYVYEISQDNSLSNVPLRKDGKYTVKELYQATAIYSANAAAIAIAEIVAGSETKFVEKMNAKAKELGLTDYKFVNATGLENKDLHGHQPEGTSVNEESEVSAKDMAVLADHLITDYPEILETSSIAKTKFREGTDDEMDMPNWNFMLKGLVSEYKKATVDGLKTGSTDSAGSCFTGTAERNGMRVITVVLNAKGNLHTGRFDETKKMFDYAFDNFSMKEIYAEGDQVKGHKTISVDKGKEKEVGIVTNKAFSLPVKNGEEKNYKAKVTLNKDNLTAPVKKGTKVGKLTAEYTGDEKDYGFLNSDLAGVDLVTKENVEKANWFVLTMRSIGGFFAGIWGSIVDTVTGWF |
| Enzyme Length | 443 |
| Uniprot Accession Number | P08750 |
| Absorption | |
| Active Site | ACT_SITE 67; /note=Acyl-ester intermediate; /evidence=ECO:0000269|PubMed:111240; ACT_SITE 70; /note=Proton acceptor; /evidence=ECO:0000250; ACT_SITE 131; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 258; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; |
| DNA Binding | |
| EC Number | 3.4.16.4 |
| Enzyme Function | FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. |
| nucleotide Binding | |
| Features | Active site (3); Binding site (1); Chain (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Carboxypeptidase;Cell membrane;Cell shape;Cell wall;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Membrane;Peptidoglycan synthesis;Protease;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall. Cell membrane {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}. Membrane raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456}. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion. {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000269|PubMed:6768745 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,636 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |