ID NAGZ_NEIMB Reviewed; 361 AA. AC Q9K0Q4; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 125. 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=NMB0530; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M., RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., RA Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(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}. 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; AE002098; AAF40960.1; -; Genomic_DNA. DR PIR; B81190; B81190. DR RefSeq; NP_273575.1; NC_003112.2. DR RefSeq; WP_002225592.1; NC_003112.2. DR AlphaFoldDB; Q9K0Q4; -. DR SMR; Q9K0Q4; -. DR STRING; 122586.NMB0530; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR PaxDb; 122586-NMB0530; -. DR KEGG; nme:NMB0530; -. DR PATRIC; fig|122586.8.peg.674; -. DR HOGENOM; CLU_008392_0_0_4; -. DR InParanoid; Q9K0Q4; -. DR OrthoDB; 9786661at2; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000000425; 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; IBA:GO_Central. 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..361 FT /note="Beta-hexosaminidase" FT /id="PRO_0000210791" 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; 39153 MW; 3E066E5B9809033A CRC64; MTVPHIPRGP VMADIAAFRL TEEEKQRLLD PAVGGIILFR RNFQNIEQLK TLTAEIKALR TPELIIAVDH EGGRVQRFIE GFTRLPAMST LGEIWDKDGA SAAETAAGQV GRVLATELSA CGIDLSFTPV LDLDWGNCPV IGNRSFHRNP EAVARLALAL QKGLTKGGMK SCGKHFPGHG FVEGDSHLVL PEDWRSLSEL ETADLAPFRI MSREGMAAVM PAHVVYPQVD TKPAGFSEIW LKQILRRDIG FKGVIFSDDL TMEGACGAGG IKERARISFE AGCDIVLVCN RPDLVDELRE DFRIPDNPTL AQRWQYMANT LGSAAAQAVM QTADFQAAQA FVAGLASPQD TAGGVKVGEA F //