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 27-MAR-2024, entry version 106. 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; Pseudomonadota; 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}. 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; 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 PaxDb; 257313-BP2080; -. DR GeneID; 69601849; -. DR KEGG; bpe:BP2080; -. DR PATRIC; fig|257313.5.peg.2236; -. DR eggNOG; COG1472; Bacteria. DR HOGENOM; CLU_008392_0_0_4; -. 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; 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; 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 //