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Database: UniProt
Entry: P40406
LinkDB: P40406
Original site: P40406 
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   09-JUL-2014, entry version 108.
DE   RecName: Full=Beta-hexosaminidase;
DE            EC=3.2.1.52;
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-
RT   chlorophenylhydrazone.";
RL   Biochim. Biophys. Acta 1186:27-34(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9274029;
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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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
RT   hydrolysis by beta-N-acetylglucosaminidase and N-acetylmuramyl-L-
RT   alanine amidase.";
RL   J. Bacteriol. 192:3132-3143(2010).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH TRANSITION
RP   STATE ANALOG, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-232 AND
RP   HIS-234, 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.,
RA   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]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 18-642 IN COMPLEX WITH
RP   SUBSTRATE 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
RT   a 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
CC       peptide-linked peptidoglycan fragments, giving rise to free
CC       GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic
CC       acid-linked peptides. Cleaves muropeptides, but not peptidoglycan.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
CC       D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.8-6.2;
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (Potential).
CC       Secreted, cell wall. Note=Detected in the culture supernatant,
CC       predominantly associated with cell wall-derived particulate
CC       material. A minor proportion is detected in the soluble fraction.
CC   -!- INDUCTION: Up-regulated during the late phase of exponential
CC       growth and during stationary phase.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
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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   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   ProteinModelPortal; P40406; -.
DR   SMR; P40406; 26-642.
DR   STRING; 224308.BSU01660; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   PaxDb; P40406; -.
DR   EnsemblBacteria; CAB11942; CAB11942; BSU01660.
DR   GeneID; 938881; -.
DR   KEGG; bsu:BSU01660; -.
DR   PATRIC; 18971875; VBIBacSub10457_0171.
DR   GenoList; BSU01660; -.
DR   eggNOG; COG1472; -.
DR   HOGENOM; HOG000248527; -.
DR   KO; K01207; -.
DR   OMA; GQMLMPD; -.
DR   OrthoDB; EOG6X9MKR; -.
DR   PhylomeDB; P40406; -.
DR   BioCyc; BSUB:BSU01660-MONOMER; -.
DR   UniPathway; UPA00544; -.
DR   EvolutionaryTrace; P40406; -.
DR   GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
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; IPR001764; Glyco_hydro_3_N.
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; Complete proteome; Glycosidase;
KW   Hydrolase; Lipoprotein; Membrane; Palmitate; Peptidoglycan synthesis;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     16       Potential.
FT   CHAIN        17    642       Beta-hexosaminidase.
FT                                /FTId=PRO_0000011785.
FT   REGION      221    222       Substrate binding.
FT   ACT_SITE    234    234       Proton donor/acceptor.
FT   ACT_SITE    318    318       Nucleophile.
FT   BINDING     123    123       Substrate.
FT   BINDING     131    131       Substrate.
FT   BINDING     191    191       Substrate.
FT   SITE        232    232       Important for catalytic activity.
FT   LIPID        17     17       N-palmitoyl cysteine (Potential).
FT   LIPID        17     17       S-diacylglycerol cysteine (Potential).
FT   MUTAGEN     232    232       D->G: Strongly reduces catalytic
FT                                efficiency and enzyme activity. Slightly
FT                                increases substrate affinity.
FT   MUTAGEN     234    234       H->G: Strongly reduces catalytic
FT                                efficiency while increasing substrate
FT                                affinity.
FT   MUTAGEN     318    318       D->N: Abolishes enzyme activity.
FT   HELIX        27     40
FT   HELIX        44     50
FT   STRAND       57     59
FT   HELIX        75     84
FT   STRAND       87     90
FT   HELIX        93     95
FT   HELIX        99    112
FT   STRAND      114    116
FT   STRAND      119    122
FT   STRAND      133    135
FT   HELIX       141    147
FT   HELIX       150    167
FT   STRAND      186    188
FT   HELIX       189    191
FT   HELIX       197    213
FT   STRAND      217    223
FT   HELIX       226    228
FT   STRAND      230    232
FT   TURN        233    235
FT   STRAND      237    239
FT   HELIX       244    249
FT   HELIX       252    260
FT   STRAND      265    268
FT   TURN        274    276
FT   STRAND      280    282
FT   TURN        284    286
FT   STRAND      289    291
FT   HELIX       294    296
FT   HELIX       298    301
FT   HELIX       302    308
FT   STRAND      313    316
FT   HELIX       323    326
FT   HELIX       331    341
FT   STRAND      344    348
FT   HELIX       355    358
FT   HELIX       359    373
FT   HELIX       379    395
FT   TURN        396    401
FT   HELIX       407    417
FT   HELIX       421    434
FT   STRAND      436    440
FT   HELIX       441    443
FT   STRAND      454    461
FT   HELIX       462    477
FT   STRAND      485    490
FT   HELIX       498    506
FT   STRAND      508    514
FT   HELIX       535    537
FT   HELIX       538    552
FT   STRAND      557    561
FT   HELIX       565    570
FT   STRAND      575    579
FT   STRAND      590    592
FT   HELIX       595    603
FT   STRAND      620    622
FT   STRAND      625    628
FT   TURN        636    638
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
//
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