| IED ID | IndEnz0010000443 |
| Enzyme Type ID | esterase000443 |
| Protein Name |
Peptidoglycan-N-acetylmuramic acid deacetylase PdaA Peptidoglycan MurNAc deacetylase EC 3.5.1.- |
| Gene Name | pdaA yfjS BSU07980 |
| 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 | MKWMCSICCAAVLLAGGAAQAEAVPNEPINWGFKRSVNHQPPDAGKQLNSLIEKYDAFYLGNTKEKTIYLTFDNGYENGYTPKVLDVLKKHRVTGTFFVTGHFVKDQPQLIKRMSDEGHIIGNHSFHHPDLTTKTADQIQDELDSVNEEVYKITGKQDNLYLRPPRGVFSEYVLKETKRLGYQTVFWSVAFVDWKINNQKGKKYAYDHMIKQAHPGAIYLLHTVSRDNAEALDDAITDLKKQGYTFKSIDDLMFEKEMRLPSL |
| Enzyme Length | 263 |
| Uniprot Accession Number | O34928 |
| Absorption | |
| Active Site | ACT_SITE 73; /note=Proton acceptor; /evidence=ECO:0000250; ACT_SITE 222; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.5.1.- |
| Enzyme Function | FUNCTION: Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N-acetylchitohexaose) as a substrate. {ECO:0000269|PubMed:12374835, ECO:0000269|PubMed:14679227, ECO:0000269|PubMed:15687192}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:15687192}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (7); Chain (1); Domain (1); Helix (12); Metal binding (2); Signal peptide (1); Site (1) |
| Keywords | 3D-structure;Cell wall biogenesis/degradation;Hydrolase;Metal-binding;Reference proteome;Signal;Sporulation |
| Interact With | |
| Induction | INDUCTION: Expression is sigma G-dependent. {ECO:0000269|PubMed:12374835}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1NY1; 1W17; 1W1A; 1W1B; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 30,069 |
| Kinetics | |
| Metal Binding | METAL 124; /note=Divalent metal cation; via tele nitrogen; METAL 128; /note=Divalent metal cation; via tele nitrogen |
| Rhea ID | |
| Cross Reference Brenda |