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 01-MAY-2013, entry version 34.
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: Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides (By
CC 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; VVLHCNG; -.
DR ProtClustDB; PRK05337; -.
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: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: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; Glyco_hydro_cat; 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 ACT_SITE 248 248 By 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
//
