GenomeNet

Database: UniProt/SWISS-PROT
Entry: NAGZ_HAEPS
LinkDB: NAGZ_HAEPS
Original site: NAGZ_HAEPS 
ID   NAGZ_HAEPS              Reviewed;         340 AA.
AC   B8F5N0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   14-MAY-2014, entry version 38.
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=HAPS_1013;
OS   Haemophilus parasuis serovar 5 (strain SH0165).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=557723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH0165;
RX   PubMed=19074396; DOI=10.1128/JB.01682-08;
RA   Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA   Jin M., Jin Q., Chen H.;
RT   "Complete genome sequence of Haemophilus parasuis SH0165.";
RL   J. Bacteriol. 191:1359-1360(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001321; ACL32632.1; -; Genomic_DNA.
DR   RefSeq; YP_002475580.1; NC_011852.1.
DR   ProteinModelPortal; B8F5N0; -.
DR   STRING; 557723.HAPS_1013; -.
DR   EnsemblBacteria; ACL32632; ACL32632; HAPS_1013.
DR   GeneID; 7277081; -.
DR   KEGG; hap:HAPS_1013; -.
DR   PATRIC; 20194309; VBIHaePar127548_1011.
DR   eggNOG; COG1472; -.
DR   HOGENOM; HOG000248526; -.
DR   KO; K01207; -.
DR   OMA; LLNGFVW; -.
DR   OrthoDB; EOG6BCT06; -.
DR   BioCyc; HPAR557723:GH24-1013-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    340       Beta-hexosaminidase.
FT                                /FTId=PRO_1000133665.
FT   REGION      157    158       Substrate binding (By similarity).
FT   ACT_SITE    170    170       Proton donor/acceptor (By similarity).
FT   ACT_SITE    242    242       Nucleophile (By similarity).
FT   BINDING      60     60       Substrate (By similarity).
FT   BINDING      68     68       Substrate (By similarity).
FT   BINDING     127    127       Substrate (By similarity).
FT   SITE        168    168       Important for catalytic activity (By
FT                                similarity).
SQ   SEQUENCE   340 AA;  38363 MW;  BC39F92576C5391B CRC64;
     MLLIDLAGYE LTQEEQELLE HPLVSGLILF TRNFHDKAQL QALIKSVRQR VKKPLLITVD
     QEGGRVQRFR EGFTKLPAMQ SFLQLDRLQL AQEAGWLMSA EMFALDIDLS FAPVLDLGHC
     SKAIGDRSFG EDVATMLPVA EAFIDGMREI GMAATGKHFP GHGHVIADSH LETPFDDRPK
     ETIFNHDIQP FKQLIAKGKL SAIMPAHVIY TQCDSQPASG SSYWLKEILR KQLQFNGVIF
     SDDLGMKGAG FMGNYVERSE KALQAGCDLL LLCNEPDGVV QVLDNLKYQP TPTQKERYLS
     LMKRKQISWS ELTASPRWQQ AHQQLATLQD QWLEWKAQNA
//
DBGET integrated database retrieval system