ID   NAGZ_BACSU              Reviewed;         642 AA.
AC   P40406;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Beta-hexosaminidase;
DE            EC=3.2.1.52 {ECO:0000269|PubMed:20400549, ECO:0000269|PubMed:20826810};
DE   AltName: Full=Beta-N-acetylhexosaminidase;
DE   AltName: Full=N-acetyl-beta-glucosaminidase;
DE   AltName: Full=N-acetylglucosaminidase;
DE   AltName: Full=ORF1;
DE   Flags: Precursor;
GN   Name=nagZ; Synonyms=ybbD, yzbA; OrderedLocusNames=BSU01660;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BD99 / MS94;
RX   PubMed=8011666; DOI=10.1016/0005-2728(94)90131-7;
RA   Quirk P.G., Guffanti A.A., Clejan S., Cheng J., Krulwich T.A.;
RT   "Isolation of Tn917 insertional mutants of Bacillus subtilis that are
RT   resistant to the protonophore carbonyl cyanide m-chlorophenylhydrazone.";
RL   Biochim. Biophys. Acta 1186:27-34(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9274029; DOI=10.1099/00221287-143-8-2763;
RA   Liu H., Haga K., Yasumoto K., Ohashi Y., Yoshikawa H., Takahashi H.;
RT   "Sequence and analysis of a 31 kb segment of the Bacillus subtilis
RT   chromosome in the area of the rrnH and rrnG operons.";
RL   Microbiology 143:2763-2767(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=20400549; DOI=10.1128/jb.01256-09;
RA   Litzinger S., Duckworth A., Nitzsche K., Risinger C., Wittmann V.,
RA   Mayer C.;
RT   "Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by
RT   beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase.";
RL   J. Bacteriol. 192:3132-3143(2010).
RN   [5] {ECO:0007744|PDB:3BMX, ECO:0007744|PDB:3NVD}
RP   X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH TRANSITION STATE
RP   ANALOG, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-232 AND HIS-234,
RP   ACTIVE SITE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=168;
RX   PubMed=20826810; DOI=10.1074/jbc.m110.131037;
RA   Litzinger S., Fischer S., Polzer P., Diederichs K., Welte W., Mayer C.;
RT   "Structural and kinetic analysis of Bacillus subtilis N-
RT   acetylglucosaminidase reveals a unique Asp-His dyad mechanism.";
RL   J. Biol. Chem. 285:35675-35684(2010).
RN   [6] {ECO:0007744|PDB:4GYJ, ECO:0007744|PDB:4GYK}
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 18-642 IN COMPLEX WITH SUBSTRATE
RP   ANALOGS, ACTIVE SITE, AND MUTAGENESIS OF ASP-318.
RX   PubMed=23177201; DOI=10.1016/j.chembiol.2012.09.016;
RA   Bacik J.P., Whitworth G.E., Stubbs K.A., Vocadlo D.J., Mark B.L.;
RT   "Active site plasticity within the glycoside hydrolase NagZ underlies a
RT   dynamic mechanism of substrate distortion.";
RL   Chem. Biol. 19:1471-1482(2012).
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 muropeptides, but not peptidoglycan.
CC       {ECO:0000269|PubMed:20400549, ECO:0000269|PubMed:20826810}.
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:0000269|PubMed:20400549, ECO:0000269|PubMed:20826810};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.8-6.2. {ECO:0000269|PubMed:20826810};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC       Secreted, cell wall {ECO:0000269|PubMed:20400549}. Note=Detected in the
CC       culture supernatant, predominantly associated with cell wall-derived
CC       particulate material. A minor proportion is detected in the soluble
CC       fraction.
CC   -!- INDUCTION: Up-regulated during the late phase of exponential growth and
CC       during stationary phase. {ECO:0000269|PubMed:20400549}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; L19954; AAA64351.1; -; Genomic_DNA.
DR   EMBL; AB002150; BAA19499.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11942.1; -; Genomic_DNA.
DR   PIR; I39839; I39839.
DR   RefSeq; NP_388047.1; NC_000964.3.
DR   RefSeq; WP_003234975.1; NZ_JNCM01000030.1.
DR   PDB; 3BMX; X-ray; 1.40 A; A/B=1-642.
DR   PDB; 3LK6; X-ray; 2.88 A; A/B/C/D=27-642.
DR   PDB; 3NVD; X-ray; 1.70 A; A/B=1-642.
DR   PDB; 4GYJ; X-ray; 1.65 A; A/B=18-642.
DR   PDB; 4GYK; X-ray; 1.80 A; A/B=18-642.
DR   PDBsum; 3BMX; -.
DR   PDBsum; 3LK6; -.
DR   PDBsum; 3NVD; -.
DR   PDBsum; 4GYJ; -.
DR   PDBsum; 4GYK; -.
DR   AlphaFoldDB; P40406; -.
DR   SMR; P40406; -.
DR   STRING; 224308.BSU01660; -.
DR   DrugBank; DB08357; Diethylene glycol diethyl ether.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   PaxDb; 224308-BSU01660; -.
DR   EnsemblBacteria; CAB11942; CAB11942; BSU_01660.
DR   GeneID; 938881; -.
DR   KEGG; bsu:BSU01660; -.
DR   PATRIC; fig|224308.179.peg.172; -.
DR   eggNOG; COG1472; Bacteria.
DR   InParanoid; P40406; -.
DR   OrthoDB; 9805821at2; -.
DR   PhylomeDB; P40406; -.
DR   BioCyc; BSUB:BSU01660-MONOMER; -.
DR   BRENDA; 3.2.1.52; 658.
DR   UniPathway; UPA00544; -.
DR   EvolutionaryTrace; P40406; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
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: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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
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   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cell shape; Cell wall;
KW   Cell wall biogenesis/degradation; Glycosidase; Hydrolase; Lipoprotein;
KW   Membrane; Palmitate; Peptidoglycan synthesis; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           17..642
FT                   /note="Beta-hexosaminidase"
FT                   /id="PRO_0000011785"
FT   ACT_SITE        234
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000305|PubMed:20826810,
FT                   ECO:0000305|PubMed:23177201"
FT   ACT_SITE        318
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:20826810,
FT                   ECO:0000305|PubMed:23177201"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20826810,
FT                   ECO:0000269|PubMed:23177201"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20826810,
FT                   ECO:0000269|PubMed:23177201"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20826810,
FT                   ECO:0000269|PubMed:23177201"
FT   BINDING         221..222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20826810,
FT                   ECO:0000269|PubMed:23177201"
FT   SITE            232
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000305|PubMed:20826810"
FT   LIPID           17
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           17
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   MUTAGEN         232
FT                   /note="D->G: Strongly reduces catalytic efficiency and
FT                   enzyme activity. Slightly increases substrate affinity."
FT                   /evidence="ECO:0000269|PubMed:20826810"
FT   MUTAGEN         234
FT                   /note="H->G: Strongly reduces catalytic efficiency while
FT                   increasing substrate affinity."
FT                   /evidence="ECO:0000269|PubMed:20826810"
FT   MUTAGEN         318
FT                   /note="D->N: Abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:23177201"
FT   HELIX           27..40
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           44..50
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           75..84
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           99..112
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          119..122
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          133..135
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           141..147
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           150..167
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           189..191
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           197..213
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          217..223
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           226..228
FT                   /evidence="ECO:0007829|PDB:3LK6"
FT   STRAND          230..232
FT                   /evidence="ECO:0007829|PDB:3LK6"
FT   TURN            233..235
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:3LK6"
FT   HELIX           244..249
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           252..260
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          265..268
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   TURN            274..276
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          280..282
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   TURN            284..286
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          289..291
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           294..296
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           298..301
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           302..308
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          313..316
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           323..326
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           331..341
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          344..348
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           355..358
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           359..373
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           379..395
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   TURN            396..401
FT                   /evidence="ECO:0007829|PDB:3NVD"
FT   HELIX           407..417
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           421..434
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          436..440
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           441..443
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          454..461
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           462..477
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          485..490
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           498..506
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          508..514
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           535..537
FT                   /evidence="ECO:0007829|PDB:4GYJ"
FT   HELIX           538..552
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          557..561
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           565..570
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          575..579
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          590..592
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   HELIX           595..603
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          620..622
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   STRAND          625..628
FT                   /evidence="ECO:0007829|PDB:3BMX"
FT   TURN            636..638
FT                   /evidence="ECO:0007829|PDB:3BMX"
SQ   SEQUENCE   642 AA;  70580 MW;  DCEA93142922F13F CRC64;
     MRPVFPLILS AVLFLSCFFG ARQTEASASK RAIDANQIVN RMSLDEKLGQ MLMPDFRNWQ
     KEGESSPQAL TKMNDEVASL VKKYQFGGII LFAENVKTTK QTVQLTDDYQ KASPKIPLML
     SIDQEGGIVT RLGEGTNFPG NMALGAARSR INAYQTGSII GKELSALGIN TDFSPVVDIN
     NNPDNPVIGV RSFSSNRELT SRLGLYTMKG LQRQDIASAL KHFPGHGDTD VDSHYGLPLV
     SHGQERLREV ELYPFQKAID AGADMVMTAH VQFPAFDDTT YKSKLDGSDI LVPATLSKKV
     MTGLLRQEMG FNGVIVTDAL NMKAIADHFG QEEAVVMAVK AGVDIALMPA SVTSLKEEQK
     FARVIQALKE AVKNGDIPEQ QINNSVERII SLKIKRGMYP ARNSDSTKEK IAKAKKIVGS
     KQHLKAEKKL AEKAVTVLKN EQHTLPFKPK KGSRILIVAP YEEQTASIEQ TIHDLIKRKK
     IKPVSLSKMN FASQVFKTEH EKQVKEADYI ITGSYVVKND PVVNDGVIDD TISDSSKWAT
     VFPRAVMKAA LQHNKPFVLM SLRNPYDAAN FEEAKALIAV YGFKGYANGR YLQPNIPAGV
     MAIFGQAKPK GTLPVDIPSV TKPGNTLYPL GYGLNIKTGR PL
//