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Database: UniProt
Entry: A0A080N5M4_9BIFI
LinkDB: A0A080N5M4_9BIFI
Original site: A0A080N5M4_9BIFI 
ID   A0A080N5M4_9BIFI        Unreviewed;       989 AA.
AC   A0A080N5M4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Beta-glucosidase-related glycosidase {ECO:0000313|EMBL:KFF30794.1};
DE            EC=3.2.1.21 {ECO:0000313|EMBL:KFF30794.1};
GN   ORFNames=BBOMB_0105 {ECO:0000313|EMBL:KFF30794.1};
OS   Bifidobacterium bombi DSM 19703.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF30794.1, ECO:0000313|Proteomes:UP000028730};
RN   [1] {ECO:0000313|EMBL:KFF30794.1, ECO:0000313|Proteomes:UP000028730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF30794.1,
RC   ECO:0000313|Proteomes:UP000028730};
RX   PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA   Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA   Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA   Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT   "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL   Appl. Environ. Microbiol. 80:6290-6302(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFF30794.1}.
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DR   EMBL; ATLK01000001; KFF30794.1; -; Genomic_DNA.
DR   RefSeq; WP_044087896.1; NZ_JDTS01000010.1.
DR   AlphaFoldDB; A0A080N5M4; -.
DR   STRING; 1341695.BBOMB_0105; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 3187562at2; -.
DR   Proteomes; UP000028730; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161, ECO:0000313|EMBL:KFF30794.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028730};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        929..949
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          448..522
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   989 AA;  108679 MW;  16269DB8C751D680 CRC64;
     MLQINMADVV NVIKSLVPYL VVIGALFVAA IIISVAVNKK TVKNEGTRKL VRSETWLVAL
     IAIVAAVSAM MSGPLSTLLN NATAKKYELQ SSTVSRANKL AEDIQDESVV MLQNDDSNLP
     LASKKVNVFG WGSTNPVYGG TGSGSMSKQY PMVSMLEGMK NAGLTTNARL TKLYTDYRKD
     RPDVSMFKQD WTLPELPAKN YTPAVMNQAK SFSDQAVVVI SRIGGEGADL PRNMKAKDVT
     YKDNSKDYPD FQEGQSLLQI DKTEQDMLDT VTKNFENVTL VYNGANTLQF DFLNKYPQIK
     SVLWCPPAGQ TGFTSLGKVL AGSINPSGKT SDTFLTDLKK GNTYNNSGDF KYDNVEEFKQ
     MVTGFTGETY PVKPTFVNYT EGIYMGYKFY ETAAKEGLIN YADYVKYPFG YGLSYTKFNQ
     KMGEVSRKDG RISFDVMVTN TGTKAGKDTV EVYYNPPYTN GGIEKASANL VKFEKSKLLK
     PGETQAVKVS FKEDEMASYD EKGVKSYVLE GGDYDVSINS DSHTVLDHKN VSIHSTITYN
     SKSNTHNGDK AVATNRFDDA RGDVTYLSRA NHFANYEQAN AAPSNFSMSD KAKSEFTNLG
     NYKDKIKESP SDKMPTTGAK NNVKLADLHG KSYNDPQWDK LLDEMSVKDM DNLIANGGYG
     TVAVPSVGKV QMTDADGPAA LNNNFTKVGS IGFPSSTSVA CTWNKELATK FGELIGDMAH
     DMNVGGWYAP SQDIHRSPFS GRNFEYFSED ATLSGTIAAG QIAGAESKGV YAFMKHFALN
     DQETNRMNML CTWADEQAIR EIYLKSFEMS VKQGHASAAM SAFNYIGPTW CGANPALLKS
     VLRDEWGFKG FVLTDYFSGA GFMNADQAIR AGNDAMLATT KTSNHVNGES ASTVLAMRQA
     SKNILYAAAN SWLYEHGEPK AAVPIWRTAM YVLWVLAALL FVLLEYVAIR RFMRRRKASK
     VEAEANATIQ PVGVNESVVS QSDSSVPRR
//
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