| IED ID | IndEnz0002002631 |
| Enzyme Type ID | protease002631 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase DacB DD-carboxypeptidase DD-peptidase EC 3.4.16.4 Penicillin-binding protein 5* PBP-5* Penicillin-binding protein 5a PBP-5a |
| Gene Name | dacB BSU23190 |
| 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 | MRIFKKAVFVIMISFLIATVNVNTAHAAIDVSAKSAIIIDGASGRVLYAKDEHQKRRIASITKIMTAVLAIESGKMDQTVTVSANAVRTEGSAIYLTEGQKVKLKDLVYGLMLRSGNDAAVAIAEHVGGSLDGFVYMMNQKAEQLGMKNTRFQNPHGLDDHENHYSTAYDMAILTKYAMKLKDYQKISGTKIYKAETMESVWKNKNKLLTMLYPYSTGGKTGYTKLAKRTLVSTASKDGIDLIAVTINDPNDWDDHMKMFNYVFEHYQTYLIAKKGDIPKLKGTFYESKAFIKRDITYLLTEEEKENVKINTTLLKPKKAWEKDASKIPDIVGHMEIMFNDATIAKVPIYYENERHQKPKKQFFETFKSIFLNAAGGAKWSI |
| Enzyme Length | 382 |
| Uniprot Accession Number | P35150 |
| Absorption | |
| Active Site | ACT_SITE 60; /note=Acyl-ester intermediate; /evidence=ECO:0000250; ACT_SITE 63; /note=Proton acceptor; /evidence=ECO:0000250; ACT_SITE 115; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 220; /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; Evidence={ECO:0000305|PubMed:3933484}; |
| DNA Binding | |
| EC Number | 3.4.16.4 |
| Enzyme Function | FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors (PubMed:3933484). Required specifically for the synthesis of the spore form of peptidoglycan (cortex) (Probable). {ECO:0000269|PubMed:3933484, ECO:0000305|PubMed:3080407}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8.5. {ECO:0000269|PubMed:3933484}; |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (19); Binding site (1); Chain (1); Helix (14); Sequence conflict (1); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Carboxypeptidase;Cell shape;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Membrane;Peptidoglycan synthesis;Protease;Reference proteome;Signal;Sporulation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Forespore outer membrane {ECO:0000269|PubMed:3080407, ECO:0000269|PubMed:3933484}; Peripheral membrane protein. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000269|PubMed:1548223 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3MFD; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,081 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |