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 01-MAY-2013, entry version 33.
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: 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.
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; VVLHCNG; -.
DR ProtClustDB; PRK05337; -.
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: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 1 340 Beta-hexosaminidase.
FT /FTId=PRO_1000133665.
FT ACT_SITE 242 242 By 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
//
