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Database: UniProt/SWISS-PROT
Entry: NAGZ_ECO27
LinkDB: NAGZ_ECO27
Original site: NAGZ_ECO27 
ID   NAGZ_ECO27              Reviewed;         341 AA.
AC   B7UPC3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   14-MAY-2014, entry version 39.
DE   RecName: Full=Beta-hexosaminidase;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase;
DE   AltName: Full=N-acetyl-beta-glucosaminidase;
GN   Name=nagZ; OrderedLocusNames=E2348C_1199;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
CC       D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ
CC       subfamily.
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DR   EMBL; FM180568; CAS08747.1; -; Genomic_DNA.
DR   RefSeq; YP_002328749.1; NC_011601.1.
DR   ProteinModelPortal; B7UPC3; -.
DR   SMR; B7UPC3; 1-326.
DR   STRING; 574521.E2348C_1199; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   EnsemblBacteria; CAS08747; CAS08747; E2348C_1199.
DR   GeneID; 7061787; -.
DR   KEGG; ecg:E2348C_1199; -.
DR   PATRIC; 18341409; VBIEscCol90278_1233.
DR   eggNOG; COG1472; -.
DR   KO; K01207; -.
DR   OMA; AHDIDLS; -.
DR   OrthoDB; EOG6BCT06; -.
DR   BioCyc; ECOL574521:GJAO-1236-MONOMER; -.
DR   UniPathway; UPA00544; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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.
FT   CHAIN         1    341       Beta-hexosaminidase.
FT                                /FTId=PRO_1000133662.
FT   REGION      163    164       Substrate binding (By similarity).
FT   ACT_SITE    176    176       Proton donor/acceptor (By similarity).
FT   ACT_SITE    248    248       Nucleophile (By similarity).
FT   BINDING      62     62       Substrate (By similarity).
FT   BINDING      70     70       Substrate (By similarity).
FT   BINDING     133    133       Substrate (By similarity).
FT   SITE        174    174       Important for catalytic activity (By
FT                                similarity).
SQ   SEQUENCE   341 AA;  37572 MW;  2932C85CE886F9ED CRC64;
     MGPVMLDVEG YELDAEEREI LAHPLVGGLI LFTRNYHDPA QLRELVRQIR AASRNHLVVA
     VDQEGGRVQR FREGFTRLPA AQSFAALLGM EEGGKLAQEA GWLMASEMIA MDIDISFAPV
     LDVGHISAAI GERSYHADPQ KALAIASRFI DGMHEAGMKT TGKHFPGHGA VTADSHKETP
     CDPRPQAEIR AKDMSVFSSL IRENKLDAIM PAHVIYSDVD PRPASGSPYW LKTVLRQELG
     FDGVIFSDDL SMEGAAIMGS YAERGQASLD AGCDMILVCN NRKGAVSVLD NLSPIKAERV
     TRLYHKGSFS RQELMDSARW KAISARLNQL HERWQEEKAG H
//
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