| IED ID | IndEnz0002018998 |
| Enzyme Type ID | protease018998 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase DacB1 D,D-carboxypeptidase DacB1 DD-carboxypeptidase DD-peptidase EC 3.4.16.- |
| Gene Name | dacB1 Rv3330 |
| Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Enzyme Sequence | MAFLRSVSCLAAAVFAVGTGIGLPTAAGEPNAAPAACPYKVSTPPAVDSSEVPAAGEPPLPLVVPPTPVGGNALGGCGIITAPGSAPAPGDVSAEAWLVADLDSGAVIAARDPHGRHRPASVIKVLVAMASINTLTLNKSVAGTADDAAVEGTKVGVNTGGTYTVNQLLHGLLMHSGNDAAYALARQLGGMPAALEKINLLAAKLGGRDTRVATPSGLDGPGMSTSAYDIGLFYRYAWQNPVFADIVATRTFDFPGHGDHPGYELENDNQLLYNYPGALGGKTGYTDDAGQTFVGAANRDGRRLMTVLLHGTRQPIPPWEQAAHLLDYGFNTPAGTQIGTLIEPDPSLMSTDRNPADRQRVDPQAAARISAADALPVRVGVAVIGALIVFGLIMVARAMNRRPQH |
| Enzyme Length | 405 |
| Uniprot Accession Number | O53380 |
| Absorption | |
| Active Site | ACT_SITE 121; /note=Acyl-ester intermediate; /evidence=ECO:0000305|PubMed:25551456; ACT_SITE 124; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P0AEB2; ACT_SITE 176; /evidence=ECO:0000250|UniProtKB:P0AEB2 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the beta-lactam antibiotic meropenem. {ECO:0000305|PubMed:25551456}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.16.- |
| Enzyme Function | FUNCTION: Probably cleaves the terminal D-Ala-D-Ala dipeptide of the peptidoglycan stem peptide (Probable). Shows weak D,D-carboxypeptidase activity in vitro (PubMed:22906310). Acts on the synthetic penta-peptide substrate Penta-DAP (L-Ala-gamma-D-Gln-DAP-D-Ala-D-Ala) (PubMed:22906310). The catalytic domain binds weakly to peptidoglycan in vitro (PubMed:25551456). {ECO:0000269|PubMed:22906310, ECO:0000269|PubMed:25551456, ECO:0000305|PubMed:22906310}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000305}. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (12); Chain (1); Helix (12); Modified residue (1); Mutagenesis (1); Signal peptide (1); Transmembrane (1); Turn (2) |
| Keywords | 3D-structure;Carboxypeptidase;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Hydrolase;Membrane;Peptidoglycan synthesis;Phosphoprotein;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. |
| Modified Residue | MOD_RES 336; /note=Phosphothreonine; by PknH; /evidence=ECO:0000269|PubMed:17286964 |
| Post Translational Modification | PTM: Phosphorylated on Thr-336 by PknH. {ECO:0000269|PubMed:17286964}. |
| Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4PPR; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,682 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |