| IED ID | IndEnz0002006247 |
| Enzyme Type ID | protease006247 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase DacD DD-carboxypeptidase DD-peptidase EC 3.4.16.4 Penicillin-binding protein 6b PBP-6b |
| Gene Name | dacD phsE yeeC b2010 JW5329 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MKRRLIIAASLFVFNLSSGFAAENIPFSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHLKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLPKAEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSRLSDYFHHKA |
| Enzyme Length | 388 |
| Uniprot Accession Number | P33013 |
| Absorption | |
| Active Site | ACT_SITE 63; /note=Acyl-ester intermediate; /evidence=ECO:0000250; ACT_SITE 66; /note=Proton acceptor; /evidence=ECO:0000250; ACT_SITE 129; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 232; /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); Erroneous initiation (1); Helix (12); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Carboxypeptidase;Cell inner membrane;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Hydrolase;Membrane;Peptidoglycan synthesis;Protease;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=N-terminal lies in the periplasmic space. {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5FSR; |
| Mapped Pubmed ID | 12444970; 12644487; 15466028; 16855223; 27329754; |
| Motif | |
| Gene Encoded By | |
| Mass | 43,346 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |