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Database: UniProt
Entry: Q8PB42
LinkDB: Q8PB42
Original site: Q8PB42 
ID   NAGZ_XANCP              Reviewed;         331 AA.
AC   Q8PB42;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   29-OCT-2014, entry version 81.
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=XCC1283;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 /
OS   LMG 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
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. {ECO:0000255|HAMAP-Rule:MF_00364}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
CC       D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
CC       {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
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00364}.
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DR   EMBL; AE008922; AAM40581.1; -; Genomic_DNA.
DR   RefSeq; NP_636657.1; NC_003902.1.
DR   ProteinModelPortal; Q8PB42; -.
DR   STRING; 190485.XCC1283; -.
DR   EnsemblBacteria; AAM40581; AAM40581; XCC1283.
DR   GeneID; 1001675; -.
DR   KEGG; xcc:XCC1283; -.
DR   PATRIC; 24073315; VBIXanCam115730_1374.
DR   eggNOG; COG1472; -.
DR   HOGENOM; HOG000248526; -.
DR   KO; K01207; -.
DR   OMA; AHDIDLS; -.
DR   OrthoDB; EOG6BCT06; -.
DR   BioCyc; XCAM190485:GIXZ-1282-MONOMER; -.
DR   UniPathway; UPA00544; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-HAMAP.
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; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.300; -; 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; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Glycosidase; Hydrolase; Peptidoglycan synthesis; Reference proteome.
FT   CHAIN         1    331       Beta-hexosaminidase.
FT                                /FTId=PRO_0000210803.
FT   REGION      163    164       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00364}.
FT   ACT_SITE    176    176       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00364}.
FT   ACT_SITE    247    247       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00364}.
FT   BINDING      60     60       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00364}.
FT   BINDING      68     68       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00364}.
FT   BINDING     133    133       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00364}.
FT   SITE        174    174       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00364}.
SQ   SEQUENCE   331 AA;  34516 MW;  0A1036216FD88174 CRC64;
     MLLIGVAGTE LSAQERDWLQ HDAVAGVVLF KRNFASRTQV AELSAAIRAA APRPQLICVD
     QEGGRVQRFR EGYSALAPLQ SFGALYATDP EGALAQARAH AQLMASEVRA SGVDLSFAPV
     VDLARGNRAI GDRAFSDDPQ VVASFTRAYV QALHAAGMGA TLKHFPGHGT VLEDTHVDHA
     SDPRPLDVLL AEDLVPFVAG IDAGADAVMM AHVVYPQVAP EPAGYASRWI EQILRGQLGF
     RGVVFSDDIG MAASFSAGGV AGRVHAHLDA GCDVVLVCHP ELVAESLQAV AGRTLNTAAL
     IGLIGRGALG WDGLLADAPT TSLSASFGTL A
//
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