ID   NAGZ_NEIMA              Reviewed;         361 AA.
AC   Q9JVT3; A1IQD2;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 123.
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};
GN   OrderedLocusNames=NMA0708;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM07963.1; -; Genomic_DNA.
DR   PIR; H81913; H81913.
DR   RefSeq; WP_002236746.1; NC_003116.1.
DR   AlphaFoldDB; Q9JVT3; -.
DR   SMR; Q9JVT3; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   EnsemblBacteria; CAM07963; CAM07963; NMA0708.
DR   KEGG; nma:NMA0708; -.
DR   HOGENOM; CLU_008392_0_0_4; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000000626; 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; Glycoside hydrolase, family 3, N-terminal domain; 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   PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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.
FT   CHAIN           1..361
FT                   /note="Beta-hexosaminidase"
FT                   /id="PRO_0000210790"
FT   ACT_SITE        187
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   ACT_SITE        258
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         174..175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   SITE            185
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
SQ   SEQUENCE   361 AA;  39023 MW;  174F048B59CAAFBC CRC64;
     MTVPCIPRGP VMADIAAFRL TEEEKQRLLD PAVGGVILFR RNFQNIAQLK ELTAEIKALR
     TPELIIAVDH EGGRVQRFIE GFTRLPAMNV LGQIWDKDGA SAAETAARQI GWVLATELSA
     CGIDLSFTPV LDLDWGNCAV IGNRSFHRNP EAVARLALAL QKGLEKGGMK SCGKHFPGHG
     FVEGDSHLVL PEDGRSLSEL EAADLAPFRI MSREGMAAVM PAHVVYPQVD TKPAGFSEIW
     LKQILRRDIG FKGVIFSDDL TMEGACGAGG IKERARISFE AGCDIVLVCN RPDLVDELRD
     DFRIPDNPAL AQRWQYMANT LGSAAAQAVI QTADFQAAQA FVAGLASPQD TAGGVKVGEA
     F
//