IED ID | IndEnz0002018841 |
Enzyme Type ID | protease018841 |
Protein Name |
Zinc D-Ala-D-Ala carboxypeptidase EC 3.4.17.14 D-alanyl-D-alanine carboxypeptidase Metallo DD-peptidase Zn DD-peptidase |
Gene Name | |
Organism | Streptomyces albus G |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces albus Streptomyces albus G |
Enzyme Sequence | MRPRPIRLLLTALVGAGLAFAPVSAVAAPTATASASADVGALDGCYTWSGTLSEGSSGEAVRQLQIRVAGYPGTGAQLAIDGQFGPATKAAVQRFQSAYGLAADGIAGPATFNKIYQLQDDDCTPVNFTYAELNRCNSDWSGGKVSAATARANALVTMWKLQAMRHAMGDKPITVNGGFRSVTCNSNVGGASNSRHMYGHAADLGAGSQGFCALAQAARNHGFTEILGPGYPGHNDHTHVAGGDGRFWSAPSCGI |
Enzyme Length | 255 |
Uniprot Accession Number | P00733 |
Absorption | |
Active Site | ACT_SITE 234; /note=Proton donor; /evidence=ECO:0000255 |
Activity Regulation | |
Binding Site | BINDING 180; /note=Substrate; /evidence=ECO:0000255 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of the bond: (Ac)(2)-L-lysyl-D-alanyl-|-D-alanine.; EC=3.4.17.14; |
DNA Binding | |
EC Number | 3.4.17.14 |
Enzyme Function | FUNCTION: This enzyme catalyzes carboxypeptidation and transpeptidation reactions involved in bacterial cell wall metabolism. It effectively catalyzes the transfer of the N-alpha, N-epsilon-diacetyl-L-lysyl-D-alanyl electrophilic group of the standard tripeptide substrate N-alpha,N-epsilon-diacetyl-L-lysyl-D-alanyl-D-alanine to water. It also performs a weak beta-lactamase activity, hydrolyzing penicillin into penicilloate at a very low rate. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Beta strand (9); Binding site (1); Chain (1); Disulfide bond (3); Helix (9); Metal binding (3); Modified residue (1); Sequence conflict (2); Signal peptide (1); Turn (3) |
Keywords | 3D-structure;Carboxypeptidase;Cell wall biogenesis/degradation;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | MOD_RES 43; /note=Blocked amino end (Asp) |
Post Translational Modification | PTM: The N-terminus is partially blocked as a result of the cyclization of the first two amino acids into anhydroaspartylglycine imide. |
Signal Peptide | SIGNAL 1..42; /evidence=ECO:0000269|PubMed:6825689 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1LBU; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 26,190 |
Kinetics | |
Metal Binding | METAL 196; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:6825689; METAL 237; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:6825689; METAL 239; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:6825689 |
Rhea ID | |
Cross Reference Brenda |