A0A0H3GDH9 · PGDA_LISM4

Function

function

Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan (PG). Deacetylates also N-acetylated PG. Does not deacetylate N-acetylmuramic acid (By similarity).
Confers host lysozyme resistance. Critical for virulence and escape from innate immune response of the host (PubMed:21768286, PubMed:25157076).
Required for intracellular survival of bacteria in macrophages of the host. Required for successful host colonization. Controls the production of inflammatory mediators in the bone marrow derived macrophages (BMMs) of the infected mouse (PubMed:21768286).
Suppresses Toll-like receptor 2 (TLR2)-dependent secretion of interleukin 6 (IL-6) and interferon-beta (IFN-beta) in the macrophages of the infected mouse. May decrease accessibility of pattern recognition receptors (PRRs) such as nucleotide-binding oligomerization domain protein (NOD) 1 of the host to the bacterial cell wall components (By similarity).
Protects cells from autolysis induced by lysozyme or by other autolysis-inducing agents (By similarity).

Catalytic activity

  • peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate.
    EC:3.5.1.104 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Features

Showing features for active site, binding site, site.

TypeIDPosition(s)Description
Active site273Proton acceptor
Binding site274Zn2+ (UniProtKB | ChEBI)
Binding site324Zn2+ (UniProtKB | ChEBI)
Binding site328Zn2+ (UniProtKB | ChEBI)
Binding site365substrate
Site389Raises pKa of active site His
Active site415Proton donor

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular ComponentGram-positive-bacterium-type cell wall
Cellular Componentplasma membrane
Molecular Functionlysozyme inhibitor activity
Molecular FunctionN-acetylglucosamine deacetylase activity
Molecular Functionprotein homodimerization activity
Molecular Functionzinc ion binding
Biological Processautolysis
Biological Processcarbohydrate metabolic process
Biological Processcell wall modification
Biological Processevasion of host immune response
Biological Processsymbiont-mediated evasion of host innate immune response

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptidoglycan-N-acetylglucosamine deacetylase PgdA
  • EC number
  • Short names
    Peptidoglycan GlcNAc deacetylase
  • Alternative names
    • N-acetylglucosamine deacetylase Pgd
    • Peptidoglycan N-deacetylase
      (PG N-deacetylase
      )
    • Petptidoglycan deacetylase
      (PG deacetylase
      )

Gene names

    • Name
      pgdA
    • Ordered locus names
      LMRG_00107

Organism names

Accessions

  • Primary accession
    A0A0H3GDH9

Proteomes

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-5Cytoplasmic
Transmembrane6-26Helical
Topological domain27-466Extracellular

Keywords

Phenotypes & Variants

Disruption phenotype

Cells lacking this gene have increased lysozyme sensitivity (PubMed:21768286, PubMed:25157076).
The growth is inhibited by 100 ug/ml hen egg white lysozyme in broth culture and the optical density of the culture is decreased, indicative of bacteriolysis. Bacterial colony-forming unit (CFU) is decreased by 2 logs in the liver and spleen of the intravenously Listeria-infected mouse. Mutant bacterial cells have intracellular growth defects in the bone marrow derived macrophages (BMMs) of the infected mouse, and increased vacuolar and cytosolic expression of cytokines interleukin 12 (IL-12), IL-1 beta and IFN-beta by the BMMs. Mutant cells undergo increased bacteriolysis in the cytosol of the BMMs leading to IL-1 beta secretion and AIM2 inflammasome-dependent pyroptosis of the infected host macrophages via the PYCARD (ASC)-dependent pathway. Double pgdA/oatA deletion mutants are more lysozyme sensitive than the single deletion mutant of this gene. Both the single and double mutant phenotypes can be rescued by lysozyme-deficient macrophages. The addition of extracellular lysozyme to the lysozyme-deficient macrophages infected by the mutants restores normal function of the BMMs (PubMed:21768286).
Exhibits attenuated virulence in mice. Killed within 30 minutes of intravenous infection in the blood of infected mice. Is as resistant as wild-type bacteria to beta-lactam antibiotics cefuroxime and penicillin G, and to and cathelin-related antimicrobial peptide (CAMP) treatment. Not killed by antimicrobial cationic peptides (PubMed:25157076).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004520921-466Peptidoglycan-N-acetylglucosamine deacetylase PgdA

Expression

Induction

Transcriptionally up-regulated by response regulator DegU and abundant non-coding RNA encoded by rli31.

Interaction

Subunit

Homodimer. Interacts (via transmembrane domain) with PbpA1 (via transmembrane domain); the interaction is important for the peptidoglycan N-deacetylase function of this protein.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain266-440NodB homology

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    466
  • Mass (Da)
    52,496
  • Last updated
    2015-09-16 v1
  • Checksum
    CB0595BF9A592E17
MKIRWIRLSLVAILIIAVVFIGVIGFQKYQFSKSRNKVIMQMDRLMKDQDGGNFRRLDKKENGVEIISYIPKTTEKKDNEIIQKEIGKATDAEVKKLNRDKETQGIIFYTYQKHRMAEQAISYKAVQSEYVKEGRTKFVLKDKKDICKNIVTDAETGALLTLGEVLIKSNQTKLNLKTAVEEELIKTGDFSLKDVGNLGKIKSLVKWNQTDFEITNSEIILPVKIPGAPEPKKVKVKLADIASSVNKRYLPSSVKVPEVPKAKTNKRIALTFDDGPSSSVTPGVLDTLKRHNVKATFFVLGSSVIQNPGLVKRELEEGHQVGSHSWDHPQLTKQSTQEVYNQILKTQKAVFDQTGYFPTTMRPPYGAVNKQVAEEIGLPIIQWSVDTEDWKYRNAGIVTKKVLAGATDGAIVLMHDIHKTTAASLDTTLTKLKSQGYEFVTIDELYGEKLQIGKQYFDKTDSRMVK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002002
EMBL· GenBank· DDBJ
AEO05427.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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