PGDAE_HELPG
ID PGDAE_HELPG Reviewed; 293 AA.
AC B5ZA76;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Peptidoglycan deacetylase;
DE Short=PG deacetylase;
DE EC=3.5.1.-;
DE AltName: Full=Acetylxylan esterase;
DE EC=3.1.1.72;
GN Name=pgdA; OrderedLocusNames=HPG27_289;
OS Helicobacter pylori (strain G27).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27;
RX PubMed=18952803; DOI=10.1128/jb.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=G27;
RX PubMed=21559431; DOI=10.1371/journal.pone.0019207;
RA Shaik M.M., Cendron L., Percudani R., Zanotti G.;
RT "The structure of Helicobacter pylori HP0310 reveals an atypical
RT peptidoglycan deacetylase.";
RL PLoS ONE 6:E19207-E19207(2011).
CC -!- FUNCTION: Catalyzes the N-deacetylation of peptidoglycan (PG), an
CC important mechanism that appears to confer lysozyme resistance and to
CC mitigate host immune detection; this likely contributes to pathogen
CC persistence in the host. The exact nature of the residue in PG that is
CC deacetylated has not been determined. Is also able to catalyze the
CC deacetylation of acetylated xylan, and, to a lesser extent, that of
CC chitin and chitosan. Therefore, this enzyme might play a role during
CC infection, considering that xylan-containing carbohydrate structures
CC are among those commonly consumed by humans (By similarity). In vitro,
CC does not show activity on N-acetylglucosamine (GlcNAc), chitotriose
CC (GlcNAc3), some N-acetyl-dipeptides and allantoinase. {ECO:0000250,
CC ECO:0000269|PubMed:21559431}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC EC=3.1.1.72;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21559431}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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; CP001173; ACI27056.1; -; Genomic_DNA.
DR RefSeq; WP_001040423.1; NC_011333.1.
DR PDB; 3QBU; X-ray; 2.57 A; A/B/C/D=1-293.
DR PDB; 4LY4; X-ray; 2.20 A; A/B/C/D=1-293.
DR PDBsum; 3QBU; -.
DR PDBsum; 4LY4; -.
DR AlphaFoldDB; B5ZA76; -.
DR SMR; B5ZA76; -.
DR PRIDE; B5ZA76; -.
DR EnsemblBacteria; ACI27056; ACI27056; HPG27_289.
DR KEGG; hpg:HPG27_289; -.
DR HOGENOM; CLU_029940_1_0_7; -.
DR OMA; HNDFTPY; -.
DR OrthoDB; 1701876at2; -.
DR BRENDA; 3.5.1.104; 2604.
DR Proteomes; UP000001735; Chromosome.
DR GO; GO:0046555; F:acetylxylan esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10938; CE4_HpPgdA_like; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR037950; PgdA-like.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS51677; NODB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Hydrolase; Metal-binding; Polysaccharide degradation; Xylan degradation;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..293
FT /note="Peptidoglycan deacetylase"
FT /id="PRO_0000424439"
FT DOMAIN 29..276
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21559431"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21559431"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21559431"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:4LY4"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:4LY4"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 98..116
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:4LY4"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:4LY4"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4LY4"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4LY4"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 219..236
FT /evidence="ECO:0007829|PDB:4LY4"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 254..267
FT /evidence="ECO:0007829|PDB:4LY4"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:4LY4"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:4LY4"
SQ SEQUENCE 293 AA; 33734 MW; 6E0D479D83BB0498 CRC64;
MAKEILVAYG VDIDAVAGWL GSYGGEDSPD DISRGLFAGE VGIPRLLKLF KKYHLPATWF
VPGHSIETFP EQMKMIVDAG HEVGAHGYSH ENPIAMSTKQ EEDVLLKSVE LIKDLTGKAP
TGYVAPWWEF SNITNELLLK HGFKYDHSLM HNDFTPYYVR VGDSWSKIDY SLEAKDWMKP
LIRGVETNLV EIPANWYLDD LPPMMFIKKS PNSFGFVSPR DIGQMWIDQF DWVYREMDYA
VFSMTIHPDV SARPQVLLMH EKIIEHINKH EGVRWVTFNE IADDFLKRNP RKK
