ID   NAGZ_ECOLI              Reviewed;         341 AA.
AC   P75949;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   24-JAN-2024, entry version 163.
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}; Synonyms=ycfO;
GN   OrderedLocusNames=b1107, JW1093;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   CHARACTERIZATION.
RC   STRAIN=K12;
RX   PubMed=1377; DOI=10.1128/jb.125.1.324-331.1976;
RA   Yem D.W., Wu H.C.;
RT   "Purification and properties of beta-N-acetylglucosaminidase from
RT   Escherichia coli.";
RL   J. Bacteriol. 125:324-331(1976).
RN   [5]
RP   CHARACTERIZATION.
RC   STRAIN=K12;
RX   PubMed=10940025; DOI=10.1128/jb.182.17.4836-4840.2000;
RA   Cheng Q., Li H., Merdek K., Park J.T.;
RT   "Molecular characterization of the beta-N-acetylglucosaminidase of
RT   Escherichia coli and its role in cell wall recycling.";
RL   J. Bacteriol. 182:4836-4840(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       Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides.
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   -!- ACTIVITY REGULATION: Slightly inhibited by GlcNAc and N-acetylmuramic
CC       acid and strongly inhibited by N-acetylglucosaminolactone.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.7.;
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000255|HAMAP-Rule:MF_00364}.
CC   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00364}.
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DR   EMBL; U00096; AAC74191.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35914.1; -; Genomic_DNA.
DR   PIR; H64854; H64854.
DR   RefSeq; NP_415625.1; NC_000913.3.
DR   RefSeq; WP_000529320.1; NZ_SSZK01000019.1.
DR   AlphaFoldDB; P75949; -.
DR   SMR; P75949; -.
DR   BioGRID; 4259534; 56.
DR   IntAct; P75949; 8.
DR   STRING; 511145.b1107; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   jPOST; P75949; -.
DR   PaxDb; 511145-b1107; -.
DR   EnsemblBacteria; AAC74191; AAC74191; b1107.
DR   GeneID; 945671; -.
DR   KEGG; ecj:JW1093; -.
DR   KEGG; eco:b1107; -.
DR   PATRIC; fig|1411691.4.peg.1160; -.
DR   EchoBASE; EB3207; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_008392_0_0_6; -.
DR   InParanoid; P75949; -.
DR   OMA; WQMAAEM; -.
DR   OrthoDB; 9786661at2; -.
DR   PhylomeDB; P75949; -.
DR   BioCyc; EcoCyc:G6567-MONOMER; -.
DR   BioCyc; MetaCyc:G6567-MONOMER; -.
DR   UniPathway; UPA00544; -.
DR   PRO; PR:P75949; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IDA:EcoCyc.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IDA:EcoCyc.
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; IMP:EcoCyc.
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   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Cytoplasm; Glycosidase; Hydrolase; Peptidoglycan synthesis;
KW   Reference proteome.
FT   CHAIN           1..341
FT                   /note="Beta-hexosaminidase"
FT                   /id="PRO_0000210785"
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;  37595 MW;  9E50C8E4DA87C7A4 CRC64;
     MGPVMLDVEG YELDAEEREI LAHPLVGGLI LFTRNYHDPA QLRELVRQIR AASRNRLVVA
     VDQEGGRVQR FREGFTRLPA AQSFAALSGM EEGGKLAQEA GWLMASEMIA MDIDISFAPV
     LDVGHISAAI GERSYHADPQ KALAIASRFI DGMHEAGMKT TGKHFPGHGA VTADSHKETP
     CDPRPQAEIR AKDMSVFSSL IRENKLDAIM PAHVIYSDVD PRPASGSPYW LKTVLRQELG
     FDGVIFSDDL SMEGAAIMGS YAERGQASLD AGCDMILVCN NRKGAVSVLD NLSPIKAERV
     TRLYHKGSFS RQELMDSARW KAISTRLNQL HERWQEEKAG H
//