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Beta-hexosaminidase (EC 3.2.1.52) (Beta-N-acetylhexosaminidase) (N-acetyl-beta-glucosaminidase)

 S5J3L6_VIBPH            Unreviewed;       327 AA.
S5J3L6;
16-OCT-2013, integrated into UniProtKB/TrEMBL.
16-OCT-2013, sequence version 1.
25-OCT-2017, entry version 28.
RecName: Full=Beta-hexosaminidase {ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00634276};
EC=3.2.1.52 {ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00634280};
AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
Name=nagZ {ECO:0000256|HAMAP-Rule:MF_00364};
ORFNames=M634_04600 {ECO:0000313|EMBL:AGQ90163.1};
Vibrio parahaemolyticus O1:Kuk str. FDA_R31.
Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
Vibrionaceae; Vibrio.
NCBI_TaxID=1338034 {ECO:0000313|EMBL:AGQ90163.1, ECO:0000313|Proteomes:UP000014929};
[1] {ECO:0000313|EMBL:AGQ90163.1, ECO:0000313|Proteomes:UP000014929}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FDA_R31 {ECO:0000313|EMBL:AGQ90163.1};
PubMed=25814612;
Ludeke C.H., Kong N., Weimer B.C., Fischer M., Jones J.L.;
"Complete Genome Sequences of a Clinical Isolate and an Environmental
Isolate of Vibrio parahaemolyticus.";
Genome Announc. 3:0-0(2015).
-!- FUNCTION: Plays a role in peptidoglycan recycling by cleaving the
terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from
peptide-linked peptidoglycan fragments, giving rise to free
GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic
acid-linked peptides. {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634279}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
{ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00634277}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
{ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00634259}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634271}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ
subfamily. {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634275}.
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EMBL; CP006004; AGQ90163.1; -; Genomic_DNA.
RefSeq; WP_020840112.1; NC_021847.1.
EnsemblBacteria; AGQ90163; AGQ90163; M634_04600.
KEGG; vpf:M634_04600; -.
KO; K01207; -.
UniPathway; UPA00544; -.
Proteomes; UP000014929; Chromosome I.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-UniRule.
GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 3.20.20.300; -; 1.
HAMAP; MF_00364; NagZ; 1.
InterPro; IPR022956; Beta_hexosaminidase_bac.
InterPro; IPR019800; Glyco_hydro_3_AS.
InterPro; IPR001764; Glyco_hydro_3_N.
InterPro; IPR036962; Glyco_hydro_3_N_sf.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF00933; Glyco_hydro_3; 1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
3: Inferred from homology;
Cell cycle {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634262};
Cell division {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634262};
Cell shape {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634255};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634281};
Complete proteome {ECO:0000313|Proteomes:UP000014929};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634266};
Glycosidase {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00656367, ECO:0000313|EMBL:AGQ90163.1};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00656367, ECO:0000313|EMBL:AGQ90163.1};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634255}.
DOMAIN 9 291 Glyco_hydro_3.
{ECO:0000259|Pfam:PF00933}.
REGION 160 161 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00364}.
ACT_SITE 173 173 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_00364}.
ACT_SITE 243 243 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_00364}.
BINDING 62 62 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00364}.
BINDING 70 70 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00364}.
BINDING 130 130 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00364}.
SITE 171 171 Important for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00364}.
SEQUENCE 327 AA; 36043 MW; 17A0248989664991 CRC64;
MGPLWVDVAG YELTAEDKEI LEHPTVGGLI LFTRNYHDIE QLQALTQSIR KAVKRPFLIG
VDQEGGRVQR FREGFSLIPA ADEYAKHHNG EELARMGGWL MAAELIAHDI DLSFAPVLDK
GHQCKAIGNR SFGEDADTIL RYSTAYMQGM KSVGMATTGK HFPGHGGVIA DSHLETPYDE
RSDIFEQDMA IFKAQIDAGI LDAMMPAHVI FPNYDSQPAS GSEYWLKHVL RQQLGFKGLI
FSDDLTMEGA AIMGSPAERG AQAMKAGCDM LLMCNKREAQ VEVLDNLSVS TVPLADALLK
KQSFSLSDLK LSHEWKAASE AMKRLTS


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