ID A0A089PSD7_PLUGE Unreviewed; 341 AA.
AC A0A089PSD7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
DE EC=3.2.1.52 {ECO:0000256|HAMAP-Rule:MF_00364};
DE AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
DE AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
GN Name=nagZ {ECO:0000256|HAMAP-Rule:MF_00364,
GN ECO:0000313|EMBL:SUB71984.1};
GN ORFNames=ABW06_04045 {ECO:0000313|EMBL:KMK15859.1}, NCTC11434_03448
GN {ECO:0000313|EMBL:SUB71984.1};
OS Pluralibacter gergoviae (Enterobacter gergoviae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK15859.1, ECO:0000313|Proteomes:UP000036196};
RN [1] {ECO:0000313|EMBL:KMK15859.1, ECO:0000313|Proteomes:UP000036196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS81F13 {ECO:0000313|EMBL:KMK15859.1,
RC ECO:0000313|Proteomes:UP000036196};
RA Greninger A.L., Miller S.;
RT "Genome sequences of Pluralibacter gergoviae.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SUB71984.1, ECO:0000313|Proteomes:UP000254381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11434 {ECO:0000313|EMBL:SUB71984.1,
RC ECO:0000313|Proteomes:UP000254381};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in peptidoglycan recycling by cleaving the
CC terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-
CC linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-
CC acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
CC {ECO:0000256|HAMAP-Rule:MF_00364}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001231, ECO:0000256|HAMAP-
CC Rule:MF_00364};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000256|HAMAP-Rule:MF_00364}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00364}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00364}.
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DR EMBL; LDZF01000003; KMK15859.1; -; Genomic_DNA.
DR EMBL; UGTG01000002; SUB71984.1; -; Genomic_DNA.
DR RefSeq; WP_043086644.1; NZ_PDKY01000002.1.
DR STRING; 61647.LG71_18860; -.
DR GeneID; 61384601; -.
DR KEGG; pge:LG71_18860; -.
DR PATRIC; fig|61647.14.peg.301; -.
DR eggNOG; COG1472; Bacteria.
DR OrthoDB; 9786661at2; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000036196; Unassembled WGS sequence.
DR Proteomes; UP000254381; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 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; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00364};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00364};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00364};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00364};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00364};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW Rule:MF_00364};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00364};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00364}; Reference proteome {ECO:0000313|Proteomes:UP000036196}.
FT DOMAIN 10..300
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT ACT_SITE 176
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT ACT_SITE 248
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT BINDING 163..164
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT SITE 174
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
SQ SEQUENCE 341 AA; 37413 MW; D9960F5C0950C050 CRC64;
MGPVMLDVEG YELDAEEREI LAHPLVGGLI LFTRNYHDPA QLRELVRQIR SASKNHLVVA
VDQEGGRVQR FHDGFTRLPA AQSFAALLGQ EEGGQLAEEA GWLMASEMIA MDIDISFAPV
LDVGHISAAI GERSYHADPQ VALAMARRVI DGMHAAGMKT TGKHFPGHGA VTADSHKETP
HDPRAQAEIR AKDMAVFSAL ISENRLDAIM PAHVIYDDVD PRPASGSAHW LKTVLRGELG
FNGVIFSDDL SMEGAAVMGS YAERGQASLD AGCDMILVCN NRKGAVSVLD NLSPIKAERV
TKLYHKGEFT RQALRDAPRW QRVSAQLEVL HERWQAYKET H
//
