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Database: UniProt
Entry: Q7UCW4
LinkDB: Q7UCW4
Original site: Q7UCW4 
ID   NAGZ_SHIFL              Reviewed;         341 AA.
AC   Q7UCW4; Q83LH8;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   01-OCT-2014, entry version 77.
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=SF1111, S1191;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(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; AE014073; AAP16617.1; -; Genomic_DNA.
DR   EMBL; AE005674; AAN42729.1; -; Genomic_DNA.
DR   RefSeq; NP_707022.1; NC_004337.2.
DR   RefSeq; NP_836811.1; NC_004741.1.
DR   ProteinModelPortal; Q7UCW4; -.
DR   SMR; Q7UCW4; 1-325.
DR   STRING; 198214.SF1111; -.
DR   PaxDb; Q7UCW4; -.
DR   EnsemblBacteria; AAN42729; AAN42729; SF1111.
DR   EnsemblBacteria; AAP16617; AAP16617; S1191.
DR   GeneID; 1024077; -.
DR   GeneID; 1077595; -.
DR   KEGG; sfl:SF1111; -.
DR   KEGG; sfx:S1191; -.
DR   PATRIC; 18703590; VBIShiFle31049_1300.
DR   eggNOG; COG1472; -.
DR   HOGENOM; HOG000248526; -.
DR   KO; K01207; -.
DR   OMA; ADSHIAM; -.
DR   OrthoDB; EOG6BCT06; -.
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_0000210799.
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    248    248       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00364}.
FT   BINDING      62     62       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00364}.
FT   BINDING      70     70       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   341 AA;  37602 MW;  3233785CE886F9ED 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 KAISTRLNQL HERWQEEKAG H
//
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