| IED ID | IndEnz0002010326 |
| Enzyme Type ID | protease010326 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase DD-carboxypeptidase DD-peptidase EC 3.4.16.4 Penicillin-binding protein PBP |
| Gene Name | dac |
| Organism | Actinomadura sp. (strain R39) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptosporangiales Thermomonosporaceae Actinomadura unclassified Actinomadura Actinomadura sp. (strain R39) |
| Enzyme Sequence | MKQSSPEPLRPRRTGGRGGARRAAALVTIPLLPMTLLGASPALADASGARLTELREDIDAILEDPALEGAVSGVVVVDTATGEELYSRDGGEQLLPASNMKLFTAAAALEVLGADHSFGTEVAAESAPGRRGEVQDLYLVGRGDPTLSAEDLDAMAAEVAASGVRTVRGDLYADDTWFDSERLVDDWWPEDEPYAYSAQISALTVAHGERFDTGVTEVSVTPAAEGEPADVDLGAAEGYAELDNRAVTGAAGSANTLVIDRPVGTNTIAVTGSLPADAAPVTALRTVDEPAALAGHLFEEALESNGVTVKGDVGLGGVPADWQDAEVLADHTSAELSEILVPFMKFSNNGHAEMLVKSIGQETAGAGTWDAGLVGVEEALSGLGVDTAGLVLNDGSGLSRGNLVTADTVVDLLGQAGSAPWAQTWSASLPVAGESDPFVGGTLANRMRGTAAEGVVEAKTGTMSGVSALSGYVPGPEGELAFSIVNNGHSGPAPLAVQDAIAVRLAEYAGHQAPEGARMMRGPVQGSGELECSWVQAC |
| Enzyme Length | 538 |
| Uniprot Accession Number | P39045 |
| Absorption | |
| Active Site | ACT_SITE 98; /note=Acyl-ester intermediate; ACT_SITE 101; /note=Proton acceptor; ACT_SITE 347; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by benzylpenicillin, cephaloridine, ampicillin and cetiofur. {ECO:0000269|PubMed:11160090}. |
| Binding Site | BINDING 459; /note=Substrate |
| 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 (25); Binding site (1); Chain (1); Helix (17); Propeptide (1); Region (2); Sequence conflict (1); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Antibiotic resistance;Carboxypeptidase;Cell shape;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Peptidoglycan synthesis;Protease;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..49; /evidence=ECO:0000269|PubMed:1554361 |
| Structure 3D | X-ray crystallography (18) |
| Cross Reference PDB | 1W79; 1W8Q; 1W8Y; 2VGJ; 2VGK; 2WKE; 2XDM; 2XK1; 2XLN; 2Y4A; 2Y55; 2Y59; 3ZCZ; 3ZVT; 3ZVW; 4B4X; 4B4Z; 4BEN; |
| Mapped Pubmed ID | 18602645; 19919161; 20608745; 21574608; 23484909; 24900305; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,974 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.16.4; |