ID   NAGZ_NITMU              Reviewed;         349 AA.
AC   Q2Y863;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Nmul_A1761;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000255|HAMAP-Rule:MF_00364}.
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}.
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; CP000103; ABB75058.1; -; Genomic_DNA.
DR   RefSeq; WP_011381078.1; NZ_FNVK01000011.1.
DR   AlphaFoldDB; Q2Y863; -.
DR   SMR; Q2Y863; -.
DR   STRING; 323848.Nmul_A1761; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   EnsemblBacteria; ABB75058; ABB75058; Nmul_A1761.
DR   KEGG; nmu:Nmul_A1761; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_008392_0_0_4; -.
DR   OMA; WQMAAEM; -.
DR   OrthoDB; 949956at2; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000002718; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; 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   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Cytoplasm; Glycosidase; Hydrolase; Peptidoglycan synthesis;
KW   Reference proteome.
FT   CHAIN           1..349
FT                   /note="Beta-hexosaminidase"
FT                   /id="PRO_0000234919"
FT   ACT_SITE        181
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   ACT_SITE        252
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         168..169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   SITE            179
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
SQ   SEQUENCE   349 AA;  38354 MW;  23E9D42AAFCBA50C CRC64;
     MSLGPVILDI EGTQLTANDK KKLRHPLVGG VILFTRNYSS LAQLMHLTAE IHALRTPPLL
     VAVDHEGGRV QRFREDFTRL PPMRELGRIW DEHPAQARHL AHEAGYVLAA ELRAAGVDFS
     FTPVLDMDYG QSSVIRDRAF HRDPQAIAEL AHSLMSGLKS AGMAAVGKHF PGHGYIEADS
     HFEMPVDERT YAQIEMDDLI PFRKMIGFGL TGMMPAHVIY PKVDALPAGF SEVWLKKVLR
     GELGFEGCIF SDDLNMAGAA FAGNPVERAQ KALHAGCDMV LLCNNPEAAE MLLAELHWDL
     PALGVIRLAR MRGRPNPDSL VKLHENPNFV SAVEKIAGIG VRSGELPLV