NAGZ_PSEAE
ID NAGZ_PSEAE Reviewed; 332 AA.
AC Q9HZK0;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Beta-hexosaminidase {ECO:0000255|HAMAP-Rule:MF_00364};
DE EC=3.2.1.52 {ECO:0000255|HAMAP-Rule:MF_00364};
DE AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000255|HAMAP-Rule:MF_00364};
DE AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000255|HAMAP-Rule:MF_00364};
GN Name=nagZ {ECO:0000255|HAMAP-Rule:MF_00364}; OrderedLocusNames=PA3005;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=24819062; DOI=10.1089/mdr.2014.0036;
RA Borisova M., Gisin J., Mayer C.;
RT "Blocking peptidoglycan recycling in Pseudomonas aeruginosa attenuates
RT intrinsic resistance to fosfomycin.";
RL Microb. Drug Resist. 20:231-237(2014).
CC -!- FUNCTION: Plays a role in peptidoglycan recycling by cleaving the
CC terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-
CC linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-
CC acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides (By
CC similarity). Contributes to intrinsic fosfomycin resistance in
CC P.aeruginosa (PubMed:24819062). {ECO:0000255|HAMAP-Rule:MF_00364,
CC ECO:0000269|PubMed:24819062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00364};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000255|HAMAP-Rule:MF_00364, ECO:0000305|PubMed:24819062}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00364}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00364}.
CC -!- DISRUPTION PHENOTYPE: Deletion of this gene increases fosfomycin
CC sensitivity. {ECO:0000269|PubMed:24819062}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00364}.
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DR EMBL; AE004091; AAG06393.1; -; Genomic_DNA.
DR PIR; G83270; G83270.
DR RefSeq; NP_251695.1; NC_002516.2.
DR RefSeq; WP_003118092.1; NZ_QZGE01000009.1.
DR PDB; 5G1M; X-ray; 1.80 A; A/B=1-332.
DR PDB; 5G2M; X-ray; 3.00 A; A/B=1-332.
DR PDB; 5G3R; X-ray; 2.18 A; A/B=1-332.
DR PDB; 5G5K; X-ray; 3.10 A; A/B=1-332.
DR PDB; 5G5U; X-ray; 2.25 A; A/B=1-332.
DR PDB; 5G6T; X-ray; 2.15 A; A/B=1-332.
DR PDB; 5LY7; X-ray; 3.10 A; A/B=1-332.
DR PDBsum; 5G1M; -.
DR PDBsum; 5G2M; -.
DR PDBsum; 5G3R; -.
DR PDBsum; 5G5K; -.
DR PDBsum; 5G5U; -.
DR PDBsum; 5G6T; -.
DR PDBsum; 5LY7; -.
DR AlphaFoldDB; Q9HZK0; -.
DR SMR; Q9HZK0; -.
DR STRING; 287.DR97_4932; -.
DR BindingDB; Q9HZK0; -.
DR ChEMBL; CHEMBL1667674; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR PaxDb; Q9HZK0; -.
DR PRIDE; Q9HZK0; -.
DR EnsemblBacteria; AAG06393; AAG06393; PA3005.
DR GeneID; 880216; -.
DR KEGG; pae:PA3005; -.
DR PATRIC; fig|208964.12.peg.3153; -.
DR PseudoCAP; PA3005; -.
DR HOGENOM; CLU_008392_0_0_6; -.
DR InParanoid; Q9HZK0; -.
DR OMA; WQMAAEM; -.
DR PhylomeDB; Q9HZK0; -.
DR BioCyc; MetaCyc:MON-20216; -.
DR BioCyc; PAER208964:G1FZ6-3057-MON; -.
DR UniPathway; UPA00544; -.
DR PRO; PR:Q9HZK0; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.300; -; 1.
DR HAMAP; MF_00364; NagZ; 1.
DR InterPro; IPR022956; Beta_hexosaminidase_bac.
DR InterPro; IPR019800; Glyco_hydro_3_AS.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Glycosidase; Hydrolase;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..332
FT /note="Beta-hexosaminidase"
FT /id="PRO_0000210795"
FT ACT_SITE 174
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 161..162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT SITE 172
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:5G1M"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:5G1M"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:5G1M"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:5G1M"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:5G1M"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:5G5K"
FT HELIX 90..107
FT /evidence="ECO:0007829|PDB:5G1M"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5G6T"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:5G3R"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 137..153
FT /evidence="ECO:0007829|PDB:5G1M"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:5G1M"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:5G3R"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:5G1M"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:5G1M"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:5G1M"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:5G1M"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:5G1M"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:5G1M"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:5G1M"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5G1M"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:5LY7"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:5G1M"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:5G1M"
FT HELIX 316..327
FT /evidence="ECO:0007829|PDB:5G1M"
SQ SEQUENCE 332 AA; 36101 MW; BA472E62B44A097A CRC64;
MQGSLMLDIG GTWLTAEDRQ ILRHPEVGGL IIFARNIEHP AQVRELCAAI RAIRPDLLLA
VDQEGGRVQR LRQGFVRLPA MRAIADNPNA EELAEHCGWL MATEVQAVGL DLSFAPVLDL
DHQRSAVVGS RAFEGDPERA ALLAGAFIRG MHAAGMAATG KHFPGHGWAE ADSHVAIPED
ARSLEEIRRS DLVPFARLAG QLDALMPAHV IYPQVDPQPA GFSRRWLQEI LRGELKFDGV
IFSDDLSMAG AHVVGDAASR IEAALAAGCD MGLVCNDRAS AELALAALQR LKVTPPSRLQ
RMRGKGYANT DYRQQPRWLE ALSALRAAQL ID
