| IED ID | IndEnz0002004975 |
| Enzyme Type ID | protease004975 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase DD-carboxypeptidase DD-peptidase EC 3.4.16.4 |
| Gene Name | |
| Organism | Streptomyces sp. (strain R61) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces unclassified Streptomyces Streptomyces sp. (strain R61) |
| Enzyme Sequence | MVSGTVGRGTALGAVLLALLAVPAQAGTAAAADLPAPDDTGLQAVLHTALSQGAPGAMVRVDDNGTIHQLSEGVADRATGRAITTTDRFRVGSVTKSFSAVVLLQLVDEGKLDLDASVNTYLPGLLPDDRITVRQVMSHRSGLYDYTNDMFAQTVPGFESVRNKVFSYQDLITLSLKHGVTNAPGAAYSYSNTNFVVAGMLIEKLTGHSVATEYQNRIFTPLNLTDTFYVHPDTVIPGTHANGYLTPDEAGGALVDSTEQTVSWAQSAGAVISSTQDLDTFFSALMSGQLMSAAQLAQMQQWTTVNSTQGYGLGLRRRDLSCGISVYGHTGTVQGYYTYAFASKDGKRSVTALANTSNNVNVLNTMARTLESAFCGKPTTAKLRSATSSATTVERHEDIAPGIARD |
| Enzyme Length | 406 |
| Uniprot Accession Number | P15555 |
| Absorption | |
| Active Site | ACT_SITE 93; /note="Acyl-ester intermediate"; /evidence="ECO:0000269|PubMed:12215418, ECO:0000269|PubMed:12564922, ECO:0000269|PubMed:15581896" |
| Activity Regulation | |
| Binding Site | BINDING 316; /note="Substrate"; /evidence="ECO:0000269|PubMed:12215418, ECO:0000269|PubMed:12564922, ECO:0000269|PubMed:15581896" |
| 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: Catalyzes distinct carboxypeptidation and transpeptidation reactions during the last stages of wall peptidoglycan synthesis. Mistaking a beta-lactam antibiotic molecule for a normal substrate (i.e. a D-alanyl-D-alanine-terminated peptide), it becomes immobilized in the form of a long-lived, serine-ester-linked acyl enzyme and thus behave as penicillin-binding protein (PBP). |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (13); Binding site (1); Chain (1); Helix (14); Propeptide (1); Region (5); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Carboxypeptidase;Cell shape;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Peptidoglycan synthesis;Protease;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31 |
| Structure 3D | X-ray crystallography (15) |
| Cross Reference PDB | 1CEF; 1CEG; 1HVB; 1IKG; 1IKI; 1MPL; 1PW1; 1PW8; 1PWC; 1PWD; 1PWG; 1SCW; 1SDE; 1YQS; 3PTE; |
| Mapped Pubmed ID | 11171967; 15170342; 15909988; 7626623; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,917 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.16.4; |