| IED ID | IndEnz0002007491 |
| Enzyme Type ID | protease007491 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase DacC DD-carboxypeptidase DD-peptidase EC 3.4.16.4 Penicillin-binding protein 4a PBP-4a |
| Gene Name | dacC pbp BSU18350 |
| 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 | MKKSIKLYVAVLLLFVVASVPYMHQAALAAEKQDALSGQIDKILADHPALEGAMAGITVRSAETGAVLYEHSGDTRMRPASSLKLLTAAAALSVLGENYSFTTEVRTDGTLKGKKLNGNLYLKGKGDPTLLPSDFDKMAEILKHSGVKVIKGNLIGDDTWHDDMRLSPDMPWSDEYTYYGAPISALTASPNEDYDAGTVIVEVTPNQKEGEEPAVSVSPKTDYITIKNDAKTTAAGSEKDLTIEREHGTNTITIEGSVPVDANKTKEWISVWEPAGYALDLFKQSLKKQGITVKGDIKTGEAPSSSDVLLSHRSMPLSKLFVPFMKLSNNGHAEVLVKEMGKVKKGEGSWEKGLEVLNSTLPEFGVDSKSLVLRDGSGISHIDAVSSDQLSQLLYDIQDQSWFSAYLNSLPVAGNPDRMVGGTLRNRMKGTPAQGKVRAKTGSLSTVSSLSGYAETKSGKKLVFSILLNGLIDEEDGKDIEDQIAVILANQ |
| Enzyme Length | 491 |
| Uniprot Accession Number | P39844 |
| Absorption | |
| Active Site | ACT_SITE 81; /note=Acyl-ester intermediate; /evidence=ECO:0000305|PubMed:17582436; ACT_SITE 84; /note=Proton acceptor; /evidence=ECO:0000305|PubMed:17582436; ACT_SITE 328; /evidence=ECO:0000305|PubMed:17582436 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by cephaloridine. {ECO:0000269|PubMed:11160090}. |
| Binding Site | BINDING 174; /note=Substrate; /evidence=ECO:0000305|PubMed:17582436; BINDING 381; /note=Substrate; /evidence=ECO:0000305|PubMed:17582436 |
| 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: Catalyzes DD-carboxypeptidase and transpeptidation reactions. {ECO:0000269|PubMed:11160090}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 12. {ECO:0000269|PubMed:11160090}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (23); Binding site (2); Chain (1); Helix (19); Region (2); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Cell cycle;Cell division;Cell shape;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Membrane;Peptidoglycan synthesis;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is sigma H-dependent. {ECO:0000269|PubMed:9733705}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22882210, ECO:0000305|PubMed:9733705}. Membrane raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}. Note=May be anchored in the membrane via a C-terminal amphipathic alpha helix. 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 (PubMed:20713508, PubMed:22882210). {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000269|PubMed:9733705 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1W5D; 2J9P; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,891 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=400 uM for N(alpha)-acetyl-L-Lys-D-Ala-D-thiolactate {ECO:0000269|PubMed:11160090}; KM=470 uM for benzoyl-Gly-thiogylcolate {ECO:0000269|PubMed:11160090}; KM=380 uM for benzoyl-D-Ala-thiogylcolate {ECO:0000269|PubMed:11160090}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.16.4; |