I6Y204 · DACB2_MYCTU
- ProteinD-alanyl-D-alanine carboxypeptidase DacB2
- GenedacB2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids291 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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).
Miscellaneous
Overexpression in Mycobacterium smegmatis results in reduced growth, an altered colony morphology, and a defect in sliding motility and biofilm formation. Overexpression of the S69C mutant shows similar results, indicating that the effects produced are independent of protein's penicillin binding function.
Activity regulation
Inhibited by the beta-lactam antibiotic meropenem (PubMed:22906310).
Inhibited by the non-specific inhibitor phenylmethylsulfonyl fluoride (PMSF) (Probable)
Inhibited by the non-specific inhibitor phenylmethylsulfonyl fluoride (PMSF) (Probable)
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 69 | Acyl-ester intermediate | ||||
Sequence: S | ||||||
Active site | 72 | Proton acceptor | ||||
Sequence: K | ||||||
Active site | 124 | |||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
Molecular Function | serine-type D-Ala-D-Ala carboxypeptidase activity | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | proteolysis | |
Biological Process | regulation of cell shape |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameD-alanyl-D-alanine carboxypeptidase DacB2
- EC number
- Short namesD,D-carboxypeptidase DacB2 ; DD-carboxypeptidase ; DD-peptidase
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionI6Y204
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Deletion of the gene results in reduced growth in acidic medium under low oxygen conditions. The mutant shows better intracellular growth and survival inside THP-1 cells compared to wild-type and complemented strains. The colony morphology and antibiotic sensitivity of mutant and wild-type strains are similar (PubMed:22138550).
The double knockout mutant pknI/dacB2 shows smoother colony morphology on solid agar and exhibits defective biofilm and cord formation. Double mutant is hypersensitive to cell wall damaging agents such as lysozyme, malachite green, ethidium bromide and to isoniazid, a first line anti-TB drug (PubMed:25467937).
The double knockout mutant pknI/dacB2 shows smoother colony morphology on solid agar and exhibits defective biofilm and cord formation. Double mutant is hypersensitive to cell wall damaging agents such as lysozyme, malachite green, ethidium bromide and to isoniazid, a first line anti-TB drug (PubMed:25467937).
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MRKLMTATAALCACAVTVSAGA | ||||||
Chain | PRO_5010244966 | 23-291 | D-alanyl-D-alanine carboxypeptidase DacB2 | |||
Sequence: AWADADVQPAGSVPIPDGPAQTWIVADLDSGQVLAGRDQNVAHPPASTIKVLLALVALDELDLNSTVVADVADTQAECNCVGVKPGRSYTARQLLDGLLLVSGNDAANTLAHMLGGQDVTVAKMNAKAATLGATSTHATTPSGLDGPGGSGASTAHDLVVIFRAAMANPVFAQITAEPSAMFPSDNGEQLIVNQDELLQRYPGAIGGKTGYTNAARKTFVGAAARGGRRLVIAMMYGLVKEGGPTYWDQAATLFDWGFALNPQASVGSL |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length291
- Mass (Da)29,747
- Last updated2012-10-03 v1
- ChecksumBE6282F8DDAFB3B8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL123456 EMBL· GenBank· DDBJ | CCP45713.1 EMBL· GenBank· DDBJ | Genomic DNA |