ID   NAGZ_SALPB              Reviewed;         341 AA.
AC   A9N5J6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
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=SPAB_02313;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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}.
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; CP000886; ABX67696.1; -; Genomic_DNA.
DR   RefSeq; WP_000529340.1; NC_010102.1.
DR   AlphaFoldDB; A9N5J6; -.
DR   SMR; A9N5J6; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   KEGG; spq:SPAB_02313; -.
DR   PATRIC; fig|1016998.12.peg.2188; -.
DR   HOGENOM; CLU_008392_0_0_6; -.
DR   BioCyc; SENT1016998:SPAB_RS09405-MONOMER; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000008556; 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..341
FT                   /note="Beta-hexosaminidase"
FT                   /id="PRO_1000079577"
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:0000255|HAMAP-Rule:MF_00364"
FT   ACT_SITE        248
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         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         163..164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   SITE            174
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
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
//