A0A0H3GDH9 · PGDA_LISM4
- ProteinPeptidoglycan-N-acetylglucosamine deacetylase PgdA
- GenepgdA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids466 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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).
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
Cofactor
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 273 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 274 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 324 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 328 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 365 | substrate | ||||
Sequence: Y | ||||||
Site | 389 | Raises pKa of active site His | ||||
Sequence: D | ||||||
Active site | 415 | Proton donor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | Gram-positive-bacterium-type cell wall | |
Cellular Component | plasma membrane | |
Molecular Function | lysozyme inhibitor activity | |
Molecular Function | N-acetylglucosamine deacetylase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | zinc ion binding | |
Biological Process | autolysis | |
Biological Process | carbohydrate metabolic process | |
Biological Process | cell wall modification | |
Biological Process | evasion of host immune response | |
Biological Process | symbiont-mediated evasion of host innate immune response |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidoglycan-N-acetylglucosamine deacetylase PgdA
- EC number
- Short namesPeptidoglycan GlcNAc deacetylase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Listeriaceae > Listeria
Accessions
- Primary accessionA0A0H3GDH9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-5 | Cytoplasmic | ||||
Sequence: MKIRW | ||||||
Transmembrane | 6-26 | Helical | ||||
Sequence: IRLSLVAILIIAVVFIGVIGF | ||||||
Topological domain | 27-466 | Extracellular | ||||
Sequence: QKYQFSKSRNKVIMQMDRLMKDQDGGNFRRLDKKENGVEIISYIPKTTEKKDNEIIQKEIGKATDAEVKKLNRDKETQGIIFYTYQKHRMAEQAISYKAVQSEYVKEGRTKFVLKDKKDICKNIVTDAETGALLTLGEVLIKSNQTKLNLKTAVEEELIKTGDFSLKDVGNLGKIKSLVKWNQTDFEITNSEIILPVKIPGAPEPKKVKVKLADIASSVNKRYLPSSVKVPEVPKAKTNKRIALTFDDGPSSSVTPGVLDTLKRHNVKATFFVLGSSVIQNPGLVKRELEEGHQVGSHSWDHPQLTKQSTQEVYNQILKTQKAVFDQTGYFPTTMRPPYGAVNKQVAEEIGLPIIQWSVDTEDWKYRNAGIVTKKVLAGATDGAIVLMHDIHKTTAASLDTTLTKLKSQGYEFVTIDELYGEKLQIGKQYFDKTDSRMVK |
Keywords
- Cellular component
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452092 | 1-466 | Peptidoglycan-N-acetylglucosamine deacetylase PgdA | |||
Sequence: MKIRWIRLSLVAILIIAVVFIGVIGFQKYQFSKSRNKVIMQMDRLMKDQDGGNFRRLDKKENGVEIISYIPKTTEKKDNEIIQKEIGKATDAEVKKLNRDKETQGIIFYTYQKHRMAEQAISYKAVQSEYVKEGRTKFVLKDKKDICKNIVTDAETGALLTLGEVLIKSNQTKLNLKTAVEEELIKTGDFSLKDVGNLGKIKSLVKWNQTDFEITNSEIILPVKIPGAPEPKKVKVKLADIASSVNKRYLPSSVKVPEVPKAKTNKRIALTFDDGPSSSVTPGVLDTLKRHNVKATFFVLGSSVIQNPGLVKRELEEGHQVGSHSWDHPQLTKQSTQEVYNQILKTQKAVFDQTGYFPTTMRPPYGAVNKQVAEEIGLPIIQWSVDTEDWKYRNAGIVTKKVLAGATDGAIVLMHDIHKTTAASLDTTLTKLKSQGYEFVTIDELYGEKLQIGKQYFDKTDSRMVK |
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.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 266-440 | NodB homology | ||||
Sequence: KRIALTFDDGPSSSVTPGVLDTLKRHNVKATFFVLGSSVIQNPGLVKRELEEGHQVGSHSWDHPQLTKQSTQEVYNQILKTQKAVFDQTGYFPTTMRPPYGAVNKQVAEEIGLPIIQWSVDTEDWKYRNAGIVTKKVLAGATDGAIVLMHDIHKTTAASLDTTLTKLKSQGYEFV |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length466
- Mass (Da)52,496
- Last updated2015-09-16 v1
- ChecksumCB0595BF9A592E17
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002002 EMBL· GenBank· DDBJ | AEO05427.1 EMBL· GenBank· DDBJ | Genomic DNA |