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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   26-NOV-2014, entry version 112.
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       {ECO:0000269|PubMed:20400549, ECO:0000269|PubMed:20826810}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
CC       D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
CC       {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-
CC       ProRule:PRU00303}. Secreted, cell wall
CC       {ECO:0000269|PubMed:20400549}. Note=Detected in the culture
CC       supernatant, predominantly associated with cell wall-derived
CC       particulate material. A minor proportion is detected in the
CC       soluble fraction.
CC   -!- INDUCTION: Up-regulated during the late phase of exponential
CC       growth and during stationary phase. {ECO:0000269|PubMed:20400549}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {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_CM000487.1.
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   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   InParanoid; P40406; -.
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-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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: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-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       {ECO:0000255|PROSITE-ProRule:PRU00303}.
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.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00303}.
FT   LIPID        17     17       S-diacylglycerol cysteine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00303}.
FT   MUTAGEN     232    232       D->G: Strongly reduces catalytic
FT                                efficiency and enzyme activity. Slightly
FT                                increases substrate affinity.
FT                                {ECO:0000269|PubMed:20826810}.
FT   MUTAGEN     234    234       H->G: Strongly reduces catalytic
FT                                efficiency while increasing substrate
FT                                affinity. {ECO:0000269|PubMed:20826810}.
FT   MUTAGEN     318    318       D->N: Abolishes enzyme activity.
FT                                {ECO:0000269|PubMed:23177201}.
FT   HELIX        27     40       {ECO:0000244|PDB:3BMX}.
FT   HELIX        44     50       {ECO:0000244|PDB:3BMX}.
FT   STRAND       57     59       {ECO:0000244|PDB:3BMX}.
FT   HELIX        75     84       {ECO:0000244|PDB:3BMX}.
FT   STRAND       87     90       {ECO:0000244|PDB:3BMX}.
FT   HELIX        93     95       {ECO:0000244|PDB:3BMX}.
FT   HELIX        99    112       {ECO:0000244|PDB:3BMX}.
FT   STRAND      114    116       {ECO:0000244|PDB:3BMX}.
FT   STRAND      119    122       {ECO:0000244|PDB:3BMX}.
FT   STRAND      133    135       {ECO:0000244|PDB:3BMX}.
FT   HELIX       141    147       {ECO:0000244|PDB:3BMX}.
FT   HELIX       150    167       {ECO:0000244|PDB:3BMX}.
FT   STRAND      186    188       {ECO:0000244|PDB:3BMX}.
FT   HELIX       189    191       {ECO:0000244|PDB:3BMX}.
FT   HELIX       197    213       {ECO:0000244|PDB:3BMX}.
FT   STRAND      217    223       {ECO:0000244|PDB:3BMX}.
FT   HELIX       226    228       {ECO:0000244|PDB:3LK6}.
FT   STRAND      230    232       {ECO:0000244|PDB:3LK6}.
FT   TURN        233    235       {ECO:0000244|PDB:3BMX}.
FT   STRAND      237    239       {ECO:0000244|PDB:3LK6}.
FT   HELIX       244    249       {ECO:0000244|PDB:3BMX}.
FT   HELIX       252    260       {ECO:0000244|PDB:3BMX}.
FT   STRAND      265    268       {ECO:0000244|PDB:3BMX}.
FT   TURN        274    276       {ECO:0000244|PDB:3BMX}.
FT   STRAND      280    282       {ECO:0000244|PDB:3BMX}.
FT   TURN        284    286       {ECO:0000244|PDB:3BMX}.
FT   STRAND      289    291       {ECO:0000244|PDB:3BMX}.
FT   HELIX       294    296       {ECO:0000244|PDB:3BMX}.
FT   HELIX       298    301       {ECO:0000244|PDB:3BMX}.
FT   HELIX       302    308       {ECO:0000244|PDB:3BMX}.
FT   STRAND      313    316       {ECO:0000244|PDB:3BMX}.
FT   HELIX       323    326       {ECO:0000244|PDB:3BMX}.
FT   HELIX       331    341       {ECO:0000244|PDB:3BMX}.
FT   STRAND      344    348       {ECO:0000244|PDB:3BMX}.
FT   HELIX       355    358       {ECO:0000244|PDB:3BMX}.
FT   HELIX       359    373       {ECO:0000244|PDB:3BMX}.
FT   HELIX       379    395       {ECO:0000244|PDB:3BMX}.
FT   TURN        396    401       {ECO:0000244|PDB:3NVD}.
FT   HELIX       407    417       {ECO:0000244|PDB:3BMX}.
FT   HELIX       421    434       {ECO:0000244|PDB:3BMX}.
FT   STRAND      436    440       {ECO:0000244|PDB:3BMX}.
FT   HELIX       441    443       {ECO:0000244|PDB:3BMX}.
FT   STRAND      454    461       {ECO:0000244|PDB:3BMX}.
FT   HELIX       462    477       {ECO:0000244|PDB:3BMX}.
FT   STRAND      485    490       {ECO:0000244|PDB:3BMX}.
FT   HELIX       498    506       {ECO:0000244|PDB:3BMX}.
FT   STRAND      508    514       {ECO:0000244|PDB:3BMX}.
FT   HELIX       535    537       {ECO:0000244|PDB:4GYJ}.
FT   HELIX       538    552       {ECO:0000244|PDB:3BMX}.
FT   STRAND      557    561       {ECO:0000244|PDB:3BMX}.
FT   HELIX       565    570       {ECO:0000244|PDB:3BMX}.
FT   STRAND      575    579       {ECO:0000244|PDB:3BMX}.
FT   STRAND      590    592       {ECO:0000244|PDB:3BMX}.
FT   HELIX       595    603       {ECO:0000244|PDB:3BMX}.
FT   STRAND      620    622       {ECO:0000244|PDB:3BMX}.
FT   STRAND      625    628       {ECO:0000244|PDB:3BMX}.
FT   TURN        636    638       {ECO:0000244|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
//
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