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Database: UniProt
Entry: Q1RK51_RICBR
LinkDB: Q1RK51_RICBR
Original site: Q1RK51_RICBR 
ID   Q1RK51_RICBR            Unreviewed;       324 AA.
AC   Q1RK51;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   OrderedLocusNames=RBE_0182 {ECO:0000313|EMBL:ABE04263.1};
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407 {ECO:0000313|EMBL:ABE04263.1, ECO:0000313|Proteomes:UP000001951};
RN   [1] {ECO:0000313|EMBL:ABE04263.1, ECO:0000313|Proteomes:UP000001951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C {ECO:0000313|EMBL:ABE04263.1,
RC   ECO:0000313|Proteomes:UP000001951};
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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DR   EMBL; CP000087; ABE04263.1; -; Genomic_DNA.
DR   RefSeq; WP_011476877.1; NC_007940.1.
DR   AlphaFoldDB; Q1RK51; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   KEGG; rbe:RBE_0182; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_008392_0_0_5; -.
DR   OrthoDB; 9786661at2; -.
DR   Proteomes; UP000001951; Chromosome.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ABE04263.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABE04263.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001951}.
FT   DOMAIN          12..311
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
SQ   SEQUENCE   324 AA;  35468 MW;  47CB3BC4664F7E90 CRC64;
     MTLEKAVKPV IIGISDTKLT DREKALLHEH SPLGIALFAR NIKTDEKGKQ NKEALAQLIT
     DIKEILGENS IIAIDQEGGR VQRLTKPTFY NAPPAKDFGD LAKDQGLEIA IEKCKQNYSN
     IGKELKALGI NLDFAPVGDI SHKGAHDVIG NRSFGTEPEI VVPLCIAALE GLQQEKVQGC
     IKHMPGHGRA KADSHKELPQ VNASIEELNE TDFKVFKELA TFNKIKLAMT AHIVYKSIDA
     NNPATLSPKV IKYIRNEIGY KGLIISDAIE MKALNGDMKD IAKKALEAGV DIVLECTGKL
     ENMIEVLDSV SKISINKFAD LLLN
//
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