(data stored in SCRATCH zone)

SWISSPROT: B4EA43_BURCJ

ID   B4EA43_BURCJ            Unreviewed;       342 AA.
AC   B4EA43;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   11-DEC-2019, entry version 77.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00345422};
DE            EC=3.2.1.52 {ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00015723};
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=nagZ1 {ECO:0000313|EMBL:CAR53159.1};
GN   Synonyms=nagZ {ECO:0000256|HAMAP-Rule:MF_00364}, nagZ2
GN   {ECO:0000313|EMBL:CAR51317.1};
GN   ORFNames=BCAL1010 {ECO:0000313|EMBL:CAR51317.1}, BCAL2860
GN   {ECO:0000313|EMBL:CAR53159.1};
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR53159.1, ECO:0000313|Proteomes:UP000001035};
RN   [1] {ECO:0000313|EMBL:CAR53159.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=J2315 {ECO:0000313|EMBL:CAR53159.1};
RA   Murnane C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAR53159.1, ECO:0000313|Proteomes:UP000001035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC   CF5610 {ECO:0000313|Proteomes:UP000001035}, and J2315
RC   {ECO:0000313|EMBL:CAR53159.1};
RX   PubMed=18931103; DOI=10.1128/JB.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(2009).
RN   [3] {ECO:0000213|PDB:4G6C}
RP   X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS).
RG   Seattle Structural Genomics Center for Infectious Disease (SSGCID);
RA   Davies D.R., Abendroth J., Staker B., Stewart L.;
RT   "Crystal structure of beta-hexosaminidase 1 from Burkholderia cenocepacia
RT   J2315.";
RL   Submitted (JUL-2012) to the PDB data bank.
RN   [4] {ECO:0000213|PDB:4GNV}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH
RP   N-ACETYL-D-GLUCOSAMINE.
RA   Davies D.R., Abendroth J., Staker B., Stewart L.;
RT   "Crystal structure of beta-hexosaminidase 1 from Burkholderia cenocepacia
RT   J2315 with bound N-Acetyl-D-Glucosamine.";
RL   Submitted (AUG-2012) to the PDB data bank.
RN   [5] {ECO:0000213|PDB:4MSS}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RX   PubMed=24136176; DOI=10.1039/c3cc46646a;
RA   Mondon M., Hur S., Vadlamani G., Rodrigues P., Tsybina P., Oliver A.,
RA   Mark B.L., Vocadlo D.J., Bleriot Y.;
RT   "Selective trihydroxyazepane NagZ inhibitors increase sensitivity of
RT   Pseudomonas aeruginosa to beta-lactams.";
RL   Chem. Commun. (Camb.) 49:10983-10985(2013).
RN   [6] {ECO:0000213|PDB:5UTP, ECO:0000213|PDB:5UTQ, ECO:0000213|PDB:5UTR}
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RX   PubMed=28370529; DOI=10.1002/pro.3166;
RA   Vadlamani G., Stubbs K.A., Desire J., Bleriot Y., Vocadlo D.J., Mark B.L.;
RT   "Conformational flexibility of the glycosidase NagZ allows it to bind
RT   structurally diverse inhibitors to suppress beta-lactam antibiotic
RT   resistance.";
RL   Protein Sci. 26:1161-1170(2017).
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, ECO:0000256|SAAS:SAAS00541113}.
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|HAMAP-Rule:MF_00364,
CC         ECO:0000256|SAAS:SAAS01118318};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00015766}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00364,
CC       ECO:0000256|SAAS:SAAS00345450}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00541107}.
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DR   EMBL; AM747720; CAR51317.1; -; Genomic_DNA.
DR   EMBL; AM747720; CAR53159.1; -; Genomic_DNA.
DR   RefSeq; WP_006485604.1; NC_011000.1.
DR   PDB; 4G6C; X-ray; 1.38 A; A/B=1-342.
DR   PDB; 4GNV; X-ray; 1.50 A; A/B=1-342.
DR   PDB; 4MSS; X-ray; 1.80 A; A/B=1-342.
DR   PDB; 5UTP; X-ray; 2.20 A; A/B=1-342.
DR   PDB; 5UTQ; X-ray; 2.20 A; A/B=1-342.
DR   PDB; 5UTR; X-ray; 2.15 A; A/B=1-342.
DR   PDBsum; 4G6C; -.
DR   PDBsum; 4GNV; -.
DR   PDBsum; 4MSS; -.
DR   PDBsum; 5UTP; -.
DR   PDBsum; 5UTQ; -.
DR   PDBsum; 5UTR; -.
DR   STRING; 216591.BCAL2860; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   EnsemblBacteria; CAR51317; CAR51317; BCAL1010.
DR   EnsemblBacteria; CAR53159; CAR53159; BCAL2860.
DR   KEGG; bcj:BCAL1010; -.
DR   KEGG; bcj:BCAL2860; -.
DR   eggNOG; ENOG4107QPA; Bacteria.
DR   eggNOG; COG1472; LUCA.
DR   HOGENOM; HOG000248526; -.
DR   KO; K01207; -.
DR   OMA; ILFARNY; -.
DR   OrthoDB; 949956at2; -.
DR   BioCyc; BCEN216591:G1G1V-1115-MONOMER; -.
DR   BioCyc; BCEN216591:G1G1V-3166-MONOMER; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000001035; Chromosome 1.
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; -; 1.
DR   HAMAP; MF_00364; NagZ; 1.
DR   InterPro; IPR022956; Beta_hexosaminidase_bac.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
DR   PRODOM; B4EA43.
DR   SWISS-2DPAGE; B4EA43.
KW   3D-structure {ECO:0000213|PDB:4G6C, ECO:0000213|PDB:4GNV,
KW   ECO:0000213|PDB:4MSS, ECO:0000213|PDB:5UTP};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00364,
KW   ECO:0000256|SAAS:SAAS00423678};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00364,
KW   ECO:0000256|SAAS:SAAS00423674};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00364,
KW   ECO:0000256|SAAS:SAAS00423670};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00364,
KW   ECO:0000256|SAAS:SAAS00423669};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00423676};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_00364,
KW   ECO:0000256|SAAS:SAAS00475007, ECO:0000313|EMBL:CAR53159.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00015732,
KW   ECO:0000313|EMBL:CAR53159.1};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00364,
KW   ECO:0000256|SAAS:SAAS00423666}.
FT   DOMAIN          10..310
FT                   /note="Glyco_hydro_3"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   REGION          170..171
FT                   /note="N-acetyl-D-glucosamine binding"
FT                   /evidence="ECO:0000213|PDB:4GNV"
FT   REGION          170..171
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   ACT_SITE        183
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   ACT_SITE        253
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   BINDING         65
FT                   /note="N-acetyl-D-glucosamine"
FT                   /evidence="ECO:0000213|PDB:4GNV"
FT   BINDING         65
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   BINDING         73
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   BINDING         140
FT                   /note="N-acetyl-D-glucosamine"
FT                   /evidence="ECO:0000213|PDB:4GNV"
FT   BINDING         140
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   BINDING         183
FT                   /note="N-acetyl-D-glucosamine"
FT                   /evidence="ECO:0000213|PDB:4GNV"
FT   BINDING         253
FT                   /note="N-acetyl-D-glucosamine"
FT                   /evidence="ECO:0000213|PDB:4GNV"
FT   BINDING         257
FT                   /note="N-acetyl-D-glucosamine"
FT                   /evidence="ECO:0000213|PDB:4GNV"
FT   SITE            181
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
SQ   SEQUENCE   342 AA;  37036 MW;  0DE33B6BE758D339 CRC64;
     MKTTPGPVML DVVGTTLSRD DARRLAHPNT GGVILFARHF QNRAQLTALT DSIRAVREDI
     LIAVDHEGGR VQRFRTDGFT VLPAMRRLGE LWDRDVLLAT KVATAVGYIL AAELRACGID
     MSFTPVLDLD YGHSKVIGDR AFHRDPRVVT LLAKSLNHGL SLAGMANCGK HFPGHGFAEA
     DSHVALPTDD RTLDAILEQD VAPYDWLGLS LAAVIPAHVI YTQVDKRPAG FSRVWLQDIL
     RGKLGFTGAI FSDDLSMEAA REGGTLTQAA DAALAAGCDM VLVCNQPDAA EVVLNGLKAR
     ASAESVRRIK RMRARGKALK WDKLIAQPEY LQAQALLSSA LA
//

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