Detail Information for IndEnz0002002630
IED ID IndEnz0002002630
Enzyme Type ID protease002630
Protein Name D-alanyl-D-alanine carboxypeptidase DacB2
D,D-carboxypeptidase DacB2
DD-carboxypeptidase
DD-peptidase
EC 3.4.16.-
Gene Name dacB2 Rv2911
Organism Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Enzyme Sequence MRKLMTATAALCACAVTVSAGAAWADADVQPAGSVPIPDGPAQTWIVADLDSGQVLAGRDQNVAHPPASTIKVLLALVALDELDLNSTVVADVADTQAECNCVGVKPGRSYTARQLLDGLLLVSGNDAANTLAHMLGGQDVTVAKMNAKAATLGATSTHATTPSGLDGPGGSGASTAHDLVVIFRAAMANPVFAQITAEPSAMFPSDNGEQLIVNQDELLQRYPGAIGGKTGYTNAARKTFVGAAARGGRRLVIAMMYGLVKEGGPTYWDQAATLFDWGFALNPQASVGSL
Enzyme Length 291
Uniprot Accession Number I6Y204
Absorption
Active Site ACT_SITE 69; /note=Acyl-ester intermediate; /evidence=ECO:0000305|PubMed:25551456; ACT_SITE 72; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P0AEB2; ACT_SITE 124; /evidence=ECO:0000250|UniProtKB:P0AEB2
Activity Regulation ACTIVITY REGULATION: Inhibited by the beta-lactam antibiotic meropenem (PubMed:22906310). Inhibited by the non-specific inhibitor phenylmethylsulfonyl fluoride (PMSF) (Probable). {ECO:0000269|PubMed:22906310, ECO:0000305|PubMed:25551456}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.16.-
Enzyme Function FUNCTION: Probably cleaves the terminal D-Ala-D-Ala dipeptide of the peptidoglycan stem peptide (Probable). Shows significant D,D-carboxypeptidase activity in vitro (PubMed:22906310). Acts on the synthetic penta-peptide substrate Penta-DAP (L-Ala-gamma-D-Gln-DAP-D-Ala-D-Ala). Shows also weak activity on Penta-Lys (L-Ala-gamma-Glu-L-Lys-D-Ala-D-Ala) (PubMed:22906310). The catalytic domain binds weakly to peptidoglycan in vitro (PubMed:25551456). Plays an important role in the maintenance of colony morphology and cell wall permeability and integrity (PubMed:25467937). {ECO:0000269|PubMed:22906310, ECO:0000269|PubMed:25467937, ECO:0000269|PubMed:25551456, ECO:0000305|PubMed:22906310}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000305|PubMed:25467937}.
nucleotide Binding
Features Active site (3); Beta strand (11); Chain (1); Helix (10); Signal peptide (1); Turn (2)
Keywords 3D-structure;Carboxypeptidase;Cell shape;Cell wall biogenesis/degradation;Hydrolase;Peptidoglycan synthesis;Periplasm;Protease;Reference proteome;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:25551456}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000255
Structure 3D X-ray crystallography (2)
Cross Reference PDB 4P0M; 4RYE;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 29,747
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda