PGDA_LISMG
ID PGDA_LISMG Reviewed; 466 AA.
AC A0A3Q0NBH7;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Peptidoglycan-N-acetylglucosamine deacetylase PgdA {ECO:0000303|PubMed:19809250};
DE Short=Peptidoglycan GlcNAc deacetylase {ECO:0000305};
DE EC=3.5.1.104 {ECO:0000269|PubMed:19809250};
DE AltName: Full=N-acetylglucosamine de-N-acetylase PgdA {ECO:0000303|PubMed:19809250};
DE AltName: Full=Peptidoglycan N-deacetylase {ECO:0000305};
DE Short=PG N-deacetylase {ECO:0000305};
DE AltName: Full=Petptidoglycan deacetylase {ECO:0000305};
DE Short=PG deacetylase {ECO:0000305};
GN Name=pgdA {ECO:0000303|PubMed:19809250};
GN ORFNames=LMON_0423 {ECO:0000312|EMBL:CDG44287.1};
OS Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1334565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGD / Mackaness;
RX PubMed=24667708; DOI=10.1128/mbio.00969-14;
RA Becavin C., Bouchier C., Lechat P., Archambaud C., Creno S., Gouin E.,
RA Wu Z., Kuhbacher A., Brisse S., Pucciarelli M.G., Garcia-del Portillo F.,
RA Hain T., Portnoy D.A., Chakraborty T., Lecuit M., Pizarro-Cerda J.,
RA Moszer I., Bierne H., Cossart P.;
RT "Comparison of widely used Listeria monocytogenes strains EGD, 10403S, and
RT EGD-e highlights genomic variations underlying differences in
RT pathogenicity.";
RL MBio 5:e00969-e00969(2014).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND 3D-STRUCTURE MODELING OF THE C-TERMINUS.
RC STRAIN=EGD / Mackaness {ECO:0000303|PubMed:19809250};
RX PubMed=19809250; DOI=10.4014/jmb.0810.557;
RA Popowska M., Kusio M., Szymanska P., Markiewicz Z.;
RT "Inactivation of the wall-associated de-N-acetylase (PgdA) of Listeria
RT monocytogenes results in greater susceptibility of the cells to induced
RT autolysis.";
RL J. Microbiol. Biotechnol. 19:932-945(2009).
CC -!- FUNCTION: Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc)
CC residues in peptidoglycan (PG). Deacetylates also N-acetylated PG. Does
CC not deacetylate N-acetylmuramic acid (PubMed:19809250). Confers host
CC lysozyme resistance. Critical for virulence and escape from innate
CC immune response of the host. Required for intracellular survival of
CC bacteria in macrophages of the host. Required for successful host
CC colonization (By similarity). Controls the production of inflammatory
CC mediators in the bone marrow derived macrophages (BMMs) of the infected
CC mouse (By similarity). Suppresses Toll-like receptor 2 (TLR2)-dependent
CC secretion of interleukin 6 (IL-6) and interferon-beta (IFN-beta) in the
CC macrophages of the infected mouse. May decrease accessibility of
CC pattern recognition receptors (PRRs) such as nucleotide-binding
CC oligomerization domain protein (NOD) 1 of the host to the bacterial
CC cell wall components (By similarity). Protects cells from autolysis
CC induced by lysozyme or by other autolysis-inducing agents
CC (PubMed:19809250). {ECO:0000250|UniProtKB:A0A0H3GDH9,
CC ECO:0000250|UniProtKB:Q8Y9V5, ECO:0000269|PubMed:19809250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-
CC glucosamine + acetate.; EC=3.5.1.104;
CC Evidence={ECO:0000269|PubMed:19809250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8DP63};
CC -!- SUBUNIT: Homodimer. Interacts (via transmembrane domain) with PbpA1
CC (via transmembrane domain); the interaction is important for the
CC peptidoglycan N-deacetylase function of this protein.
CC {ECO:0000250|UniProtKB:Q8Y9V5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8Y9V5};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q8Y9V5,
CC ECO:0000255}; Extracellular side {ECO:0000250|UniProtKB:Q8Y9V5}.
CC Secreted, cell wall {ECO:0000305|PubMed:19809250}.
CC -!- INDUCTION: Transcriptionally up-regulated by response regulator DegU
CC and abundant non-coding RNA encoded by rli31.
CC {ECO:0000250|UniProtKB:A0A0H3GDH9}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have no or very low
CC levels of de-N-acetylated sugar moieties in peptidoglycan. Mutant cells
CC have normal growth in logarithmic and stationary phases at various
CC temperatures and in different growth media and normal morphological
CC appearance. The rate of autolysis of the cell wall peptidoglycan
CC induced by EDTA, Triton-X, lysozyme or mutanolysin is significantly
CC faster and the mutant cells have a slight increase in susceptibility to
CC beta-lactam antibiotics ampicillin, penicillin and octacillin compared
CC to wild-type. {ECO:0000269|PubMed:19809250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG421741; CDG44287.1; -; Genomic_DNA.
DR RefSeq; WP_003733946.1; NC_022568.1.
DR AlphaFoldDB; A0A3Q0NBH7; -.
DR SMR; A0A3Q0NBH7; -.
DR EnsemblBacteria; CDG44287; CDG44287; LMON_0423.
DR KEGG; lmod:LMON_0423; -.
DR Proteomes; UP000016703; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009275; C:Gram-positive-bacterium-type cell wall; IC:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0060241; F:lysozyme inhibitor activity; ISS:UniProtKB.
DR GO; GO:0050119; F:N-acetylglucosamine deacetylase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0001896; P:autolysis; IMP:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0042545; P:cell wall modification; IDA:UniProtKB.
DR GO; GO:0042785; P:evasion of host immune response via regulation of host cytokine network; ISS:UniProtKB.
DR GO; GO:1903591; P:negative regulation of lysozyme activity; ISS:UniProtKB.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR017219; Peptidoglycan_deacetylase.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR PIRSF; PIRSF037479; PG_GlcNAc_deacetylase; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS51677; NODB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Hydrolase; Membrane; Metal-binding; Secreted;
KW Transmembrane; Transmembrane helix; Virulence; Zinc.
FT CHAIN 1..466
FT /note="Peptidoglycan-N-acetylglucosamine deacetylase PgdA"
FT /id="PRO_0000452094"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..466
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 266..440
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR037479-1,
FT ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 415
FT /note="Proton donor"
FT /evidence="ECO:0000255|PIRSR:PIRSR037479-1,
FT ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PIRSR:PIRSR037479-3"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PIRSR:PIRSR037479-3"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PIRSR:PIRSR037479-3"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR037479-2"
FT SITE 389
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000255|PIRSR:PIRSR037479-4"
SQ SEQUENCE 466 AA; 52496 MW; CB0595BF9A592E17 CRC64;
MKIRWIRLSL VAILIIAVVF IGVIGFQKYQ FSKSRNKVIM QMDRLMKDQD GGNFRRLDKK
ENGVEIISYI PKTTEKKDNE IIQKEIGKAT DAEVKKLNRD KETQGIIFYT YQKHRMAEQA
ISYKAVQSEY VKEGRTKFVL KDKKDICKNI VTDAETGALL TLGEVLIKSN QTKLNLKTAV
EEELIKTGDF SLKDVGNLGK IKSLVKWNQT DFEITNSEII LPVKIPGAPE PKKVKVKLAD
IASSVNKRYL PSSVKVPEVP KAKTNKRIAL TFDDGPSSSV TPGVLDTLKR HNVKATFFVL
GSSVIQNPGL VKRELEEGHQ VGSHSWDHPQ LTKQSTQEVY NQILKTQKAV FDQTGYFPTT
MRPPYGAVNK QVAEEIGLPI IQWSVDTEDW KYRNAGIVTK KVLAGATDGA IVLMHDIHKT
TAASLDTTLT KLKSQGYEFV TIDELYGEKL QIGKQYFDKT DSRMVK
