NAGZ_BORPE
ID NAGZ_BORPE Reviewed; 352 AA.
AC Q7VWV8;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=BP2080;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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; BX640417; CAE42358.1; -; Genomic_DNA.
DR RefSeq; NP_880742.1; NC_002929.2.
DR RefSeq; WP_010930725.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VWV8; -.
DR SMR; Q7VWV8; -.
DR STRING; 257313.BP2080; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR GeneID; 45389394; -.
DR KEGG; bpe:BP2080; -.
DR PATRIC; fig|257313.5.peg.2236; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_008392_0_0_4; -.
DR OMA; WQMAAEM; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000002676; 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..352
FT /note="Beta-hexosaminidase"
FT /id="PRO_0000210783"
FT ACT_SITE 192
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 179..180
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT SITE 190
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
SQ SEQUENCE 352 AA; 38622 MW; 19ECD136E3459BC5 CRC64;
MSSKKKTKPV LPPGPVMVDV AGTTLTKDEK RRLRNPLVGG VILFARNFTD RRQLCALTRA
IHKARKEPLL IAVDHEGGRV QRFRDDGFTA LPPMQELGKL WDRDPLAAMR LATEAGYVLA
AELRACGVDL SFTPVLDLDY GVSKVIGNRA FHHDARVVTM LSRALTQGLA LAGMAACGKH
FPGHGFVGAD SHHEIPVDPR PLARILKDDA APYAWLGDLV MPAVMPAHVI YPKVDAQPAG
FSRRWVSEIL RERLGYDGVV FSDDLTMEGA SVAGDILARA EAALGAGCDM VLVCRPDLAD
ELLDRLQVQH PAASVERIRR LLPRFAAPDW DTLQNDSRYQ HARRLQSQIV SG
