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Database: UniProt
Entry: Q8A798_BACTN
LinkDB: Q8A798_BACTN
Original site: Q8A798_BACTN 
ID   Q8A798_BACTN            Unreviewed;       776 AA.
AC   Q8A798;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   OrderedLocusNames=BT_1627 {ECO:0000313|EMBL:AAO76734.1};
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO76734.1, ECO:0000313|Proteomes:UP000001414};
RN   [1] {ECO:0000313|EMBL:AAO76734.1, ECO:0000313|Proteomes:UP000001414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
RN   [2] {ECO:0000313|EMBL:AAO76734.1, ECO:0000313|Proteomes:UP000001414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285}.
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DR   EMBL; AE015928; AAO76734.1; -; Genomic_DNA.
DR   RefSeq; NP_810540.1; NC_004663.1.
DR   RefSeq; WP_011107900.1; NC_004663.1.
DR   AlphaFoldDB; Q8A798; -.
DR   STRING; 226186.BT_1627; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   PaxDb; 226186-BT_1627; -.
DR   EnsemblBacteria; AAO76734; AAO76734; BT_1627.
DR   KEGG; bth:BT_1627; -.
DR   PATRIC; fig|226186.12.peg.1665; -.
DR   eggNOG; COG3525; Bacteria.
DR   HOGENOM; CLU_007082_5_0_10; -.
DR   InParanoid; Q8A798; -.
DR   OrthoDB; 1090159at2; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IBA:GO_Central.
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:0030203; P:glycosaminoglycan metabolic process; IBA:GO_Central.
DR   CDD; cd06563; GH20_chitobiase-like; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR026876; Fn3_assoc_repeat.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR015882; HEX_bac_N.
DR   PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF13287; Fn3_assoc; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001414};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..776
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004303164"
FT   DOMAIN          30..159
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          163..517
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   DOMAIN          648..751
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|Pfam:PF00754"
FT   ACT_SITE        346
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   776 AA;  87530 MW;  EF5EEB31FC29EA07 CRC64;
     MTRAILILLI GFLSSIVAGC SDTNLTHDIP LVPRPAQIVP GSGNYLFSGK TVFAVENEEQ
     AEVARSFIAL FTRAAGFTPK LTVGDAEKGN VRFQTDATLK SEAYTLQVSP KEIIIEASDA
     KGFFYALQTI RQLLPASIEK EEVSDKKVKW SIPAVSIQDE PRFGYRALLL DASRFFIPKE
     NVLRIIDCMA MLKINTLHFH LTDDNGWRVE IKKYPRLTEV GAWRVDRTDL PFPARRNPEP
     GEPTPVGGFY TQEEIKEMVA YAAERQIEVV PEIDMPAHSN SALAAYPHLA CPVVKEYIGV
     LPGLGGRNSE IIYCAGNDSV YAFLQDVMDE ILELFPSRYI HIGGDEARKT YWEKCPLCQA
     RMKKEKIANE EDLQGYFMNR MSEYVRSKGR EVIGWDELTN SSFLPDDAII LGWQGYGQAA
     LKAAEKGHRF IMTPARIMYL IRYQGPQWFE PLTYFGNNTL KDVYDYEPVQ KDWKPEYADL
     LMGVQACMWT EFCNKPEDVD YLVFPRLAAL AEVAWTQPEK KDWTSFLEGM DSFNEHLAAK
     GIVYARSMYN IQHTVRPEDG ALKVKLECVR PDVEIRYTMD GSEPTAASPL YEQPLLVKEA
     QTVNAATFAD GQQMGKTLTL PVHWNKATAK PLLGNKVNEA VLNNGVRGSL KQTDFEWCSW
     GSSDRISFTV DLLQKEKMNT LTIGCITNYG MGVHKPKSIR VAVSDDNATY RDINELEYTP
     EEIFREGTFI EDLSIDMRGT VARYVRVTTE GAGECPANHV RPGQESRVCF DELIIE
//
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