| IED ID | IndEnz0002018459 |
| Enzyme Type ID | protease018459 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase DacC DD-carboxypeptidase DD-peptidase EC 3.4.16.4 Penicillin-binding protein 6 PBP-6 |
| Gene Name | dacC b0839 JW0823 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFGRVWDFVMMKFHQWFGSWFS |
| Enzyme Length | 400 |
| Uniprot Accession Number | P08506 |
| Absorption | |
| Active Site | ACT_SITE 66; /note=Acyl-ester intermediate; /evidence=ECO:0000250; ACT_SITE 69; /note=Proton acceptor; /evidence=ECO:0000250; ACT_SITE 132; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 235; /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); Beta strand (16); Binding site (1); Chain (1); Helix (14); Region (1); Sequence conflict (1); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Carboxypeptidase;Cell inner membrane;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Membrane;Peptidoglycan synthesis;Protease;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:3330754}; Peripheral membrane protein {ECO:0000269|PubMed:3330754}; Periplasmic side {ECO:0000269|PubMed:3330754}. Note=N-terminus lies in the periplasmic space, targeted there by the C-terminal amphiphilic helix (PMID:3330754). |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000269|PubMed:7042389 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3IT9; 3ITA; 3ITB; |
| Mapped Pubmed ID | 11567017; 12644487; 1391; 1648559; 16606699; 18387365; 19807181; 319999; 6272207; 6451612; 8439290; |
| Motif | |
| Gene Encoded By | |
| Mass | 43,609 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |