IED ID | IndEnz0002018459 |
Enzyme Type ID | protease018459 |
Protein Name |
D-alanyl-D-alanine carboxypeptidase DacC DD-carboxypeptidase DD-peptidase EC 3.4.16.4 Penicillin-binding protein 6 PBP-6 |
Gene Name | dacC b0839 JW0823 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFGRVWDFVMMKFHQWFGSWFS |
Enzyme Length | 400 |
Uniprot Accession Number | P08506 |
Absorption | |
Active Site | ACT_SITE 66; /note=Acyl-ester intermediate; /evidence=ECO:0000250; ACT_SITE 69; /note=Proton acceptor; /evidence=ECO:0000250; ACT_SITE 132; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | BINDING 235; /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; |
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 (16); Binding site (1); Chain (1); Helix (14); Region (1); Sequence conflict (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 {ECO:0000269|PubMed:3330754}; Peripheral membrane protein {ECO:0000269|PubMed:3330754}; Periplasmic side {ECO:0000269|PubMed:3330754}. Note=N-terminus lies in the periplasmic space, targeted there by the C-terminal amphiphilic helix (PMID:3330754). |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000269|PubMed:7042389 |
Structure 3D | X-ray crystallography (3) |
Cross Reference PDB | 3IT9; 3ITA; 3ITB; |
Mapped Pubmed ID | 11567017; 12644487; 1391; 1648559; 16606699; 18387365; 19807181; 319999; 6272207; 6451612; 8439290; |
Motif | |
Gene Encoded By | |
Mass | 43,609 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |