NAGZ_BACSU
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 03-AUG-2022, entry version 141.
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; Firmicutes; 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; P40406; -.
DR PRIDE; P40406; -.
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 OMA; STDQEHG; -.
DR PhylomeDB; P40406; -.
DR BioCyc; BSUB:BSU01660-MON; -.
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; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 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 Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 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
