NAGZ_SALTY
ID NAGZ_SALTY Reviewed; 341 AA.
AC Q8ZQ06;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=STM1209;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH DISACCHARIDE
RP SUBSTRATE, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, AND MUTAGENESIS OF
RP ASP-248.
RX PubMed=23177201; DOI=10.1016/j.chembiol.2012.09.016;
RA Bacik J.P., Whitworth G.E., Stubbs K.A., Vocadlo D.J., Mark B.L.;
RT "Active site plasticity within the glycoside hydrolase NagZ underlies a
RT dynamic mechanism of substrate distortion.";
RL Chem. Biol. 19:1471-1482(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24009110; DOI=10.1002/cbic.201300395;
RA Stubbs K.A., Bacik J.P., Perley-Robertson G.E., Whitworth G.E.,
RA Gloster T.M., Vocadlo D.J., Mark B.L.;
RT "The development of selective inhibitors of NagZ: increased susceptibility
RT of Gram-negative bacteria to beta-lactams.";
RL ChemBioChem 14:1973-1981(2013).
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.
CC Plays a role in beta-lactam antibiotic resistance via its role in
CC generating anhydro-N-acetylmuramic acid-linked peptides; these peptides
CC function as signaling molecules that induce high-level expression of
CC the beta-lactamase AmpC. {ECO:0000255|HAMAP-Rule:MF_00364,
CC ECO:0000269|PubMed:23177201, ECO:0000269|PubMed:24009110}.
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 ECO:0000269|PubMed:23177201, ECO:0000269|PubMed:24009110};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000255|HAMAP-Rule:MF_00364}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00364}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00364}.
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DR EMBL; AE006468; AAL20138.1; -; Genomic_DNA.
DR RefSeq; NP_460179.1; NC_003197.2.
DR RefSeq; WP_000529340.1; NC_003197.2.
DR PDB; 4GVF; X-ray; 1.35 A; A/B=1-341.
DR PDB; 4GVG; X-ray; 1.70 A; A/B=1-341.
DR PDB; 4GVH; X-ray; 1.45 A; A/B=1-341.
DR PDB; 4GVI; X-ray; 1.55 A; A/B=1-341.
DR PDB; 4HZM; X-ray; 1.45 A; A/B=1-341.
DR PDBsum; 4GVF; -.
DR PDBsum; 4GVG; -.
DR PDBsum; 4GVH; -.
DR PDBsum; 4GVI; -.
DR PDBsum; 4HZM; -.
DR AlphaFoldDB; Q8ZQ06; -.
DR SMR; Q8ZQ06; -.
DR STRING; 99287.STM1209; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR PaxDb; Q8ZQ06; -.
DR EnsemblBacteria; AAL20138; AAL20138; STM1209.
DR GeneID; 1252727; -.
DR KEGG; stm:STM1209; -.
DR PATRIC; fig|99287.12.peg.1278; -.
DR HOGENOM; CLU_008392_0_0_6; -.
DR OMA; WQMAAEM; -.
DR PhylomeDB; Q8ZQ06; -.
DR BioCyc; SENT99287:STM1209-MON; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000001014; 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..341
FT /note="Beta-hexosaminidase"
FT /id="PRO_0000210797"
FT REGION 170..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:23177201"
FT ACT_SITE 248
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364,
FT ECO:0000269|PubMed:23177201"
FT BINDING 62
FT /ligand="substrate"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 133
FT /ligand="substrate"
FT BINDING 163..164
FT /ligand="substrate"
FT SITE 174
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT MUTAGEN 176
FT /note="H->G: Reduced enzyme activity."
FT MUTAGEN 248
FT /note="D->N: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:23177201"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:4GVF"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:4GVF"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:4GVF"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4GVF"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4GVF"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 83..109
FT /evidence="ECO:0007829|PDB:4GVF"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:4GVF"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 139..156
FT /evidence="ECO:0007829|PDB:4GVF"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4GVF"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:4GVF"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:4GVF"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:4GVF"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:4GVF"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 311..316
FT /evidence="ECO:0007829|PDB:4GVF"
FT HELIX 318..339
FT /evidence="ECO:0007829|PDB:4GVF"
SQ SEQUENCE 341 AA; 37698 MW; E07E83487336A300 CRC64;
MGPVMLNVEG CELDAEEREI LAHPLVGGLI LFTRNYHDPE QLRELVRQIR AASRNHLVVA
VDQEGGRVQR FREGFTRLPA AQSFFALHGL EEGGRLAQEA GWLMASEMIA MDIDISFAPV
LDVGHISAAI GERSYHADPA KALAMATRFI DGMHDAGMKT TGKHFPGHGA VTADSHKETP
CDPRPETDIR GKDMSVFRTL ISENKLDAIM PAHVIYRAID PRPASGSPYW LKTVLRQELG
FDGVIFSDDL SMEGAAIMGS YAERAQASLD AGCDMILVCN NRKGAVSVLD NLSPIKAERV
TRLYHKGSFS RRELMDSARW KTASAQLNQL HERWQEEKAG H
