| IED ID | IndEnz0002015545 |
| Enzyme Type ID | protease015545 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase DacA DD-carboxypeptidase DD-peptidase EC 3.4.16.4 Beta-lactamase EC 3.5.2.6 Penicillin-binding protein 5 PBP-5 |
| Gene Name | dacA pfv b0632 JW0627 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MNTIFSARIMKRLALTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTIGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADFAAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNSSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWFG |
| Enzyme Length | 403 |
| Uniprot Accession Number | P0AEB2 |
| Absorption | |
| Active Site | ACT_SITE 73; /note=Acyl-ester intermediate; ACT_SITE 76; /note=Proton acceptor; ACT_SITE 139 |
| Activity Regulation | |
| Binding Site | BINDING 242; /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; CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; |
| DNA Binding | |
| EC Number | 3.4.16.4; 3.5.2.6 |
| 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 (16); Mutagenesis (3); Natural variant (1); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Carboxypeptidase;Cell inner membrane;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Membrane;Peptidoglycan synthesis;Protease;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note=N-terminal lies in the periplasmic space. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000269|PubMed:7042389 |
| Structure 3D | X-ray crystallography (13) |
| Cross Reference PDB | 1HD8; 1NJ4; 1NZO; 1NZU; 1SDN; 1Z6F; 3BEB; 3BEC; 3MZD; 3MZE; 3MZF; 5J8X; 6NTZ; |
| Mapped Pubmed ID | 11112264; 14750804; 15690043; 16038617; 16606699; 17502412; 18576637; 18602645; 20726582; 2181451; 27499424; 3055172; 31015395; 319999; 3898066; 6363404; 6451612; 8162192; |
| Motif | |
| Gene Encoded By | |
| Mass | 44,444 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:20401 |
| Cross Reference Brenda | 3.4.16.4; |