| IED ID | IndEnz0002005434 |
| Enzyme Type ID | protease005434 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase DD-carboxypeptidase DD-peptidase EC 3.4.16.4 Penicillin-binding protein PBP |
| Gene Name | |
| Organism | Streptomyces sp. (strain K15) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces unclassified Streptomyces Streptomyces sp. (strain K15) |
| Enzyme Sequence | MRLRRAAATVITTGALLAAGTLGATPATAVTKPTIAAVGGYAMNNGTGTTLYTKAADTRRSTGSTTKIMTAKVVLAQSNLNLDAKVTIQKAYSDYVVANKPSQAHLIVGDKVTVRQLLYGLMLPSGCDAAYALADKYGSGSQAAARVKSFIGKMNTAATNLGLHNTHFDSFDGIGNGANYSTPRHLTKIASSAMKNSTFRTVVKTKAYTAKTVTKTGSIRTMDTWKNTNGLLSSYSGAIGVKTGSGPEAKYCLVFAATRGGKTVIGTVLASTSIPARESDATKIMNYGFAL |
| Enzyme Length | 291 |
| Uniprot Accession Number | P39042 |
| Absorption | |
| Active Site | ACT_SITE 64; /note=Acyl-ester intermediate; /evidence=ECO:0000269|PubMed:2764892; ACT_SITE 67; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:2764892; ACT_SITE 125; /evidence=ECO:0000269|PubMed:2764892 |
| 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; |
| 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 (12); Binding site (1); Chain (1); Helix (10); Mutagenesis (3); Sequence conflict (2); Signal peptide (1); Turn (2) |
| 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 {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000269|PubMed:2764892 |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 1ES2; 1ES3; 1ES4; 1ES5; 1ESI; 1J9M; 1SKF; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 30,258 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.16.4; |