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Database: UniProt
Entry: A0A1H4VPB8_9ACTN
LinkDB: A0A1H4VPB8_9ACTN
Original site: A0A1H4VPB8_9ACTN 
ID   A0A1H4VPB8_9ACTN        Unreviewed;       818 AA.
AC   A0A1H4VPB8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=SAMN04489844_3069 {ECO:0000313|EMBL:SEC82793.1};
OS   Nocardioides exalbidus.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=402596 {ECO:0000313|EMBL:SEC82793.1, ECO:0000313|Proteomes:UP000198742};
RN   [1] {ECO:0000313|Proteomes:UP000198742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22017 {ECO:0000313|Proteomes:UP000198742};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448};
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DR   EMBL; FNRT01000002; SEC82793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4VPB8; -.
DR   STRING; 402596.SAMN04489844_3069; -.
DR   Proteomes; UP000198742; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; 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; PTHR30620:SF121; PERIPLASMIC BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-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.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          737..806
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   818 AA;  86664 MW;  254C37A112E1C064 CRC64;
     MLPGERKVRY VTPALGQVPS GLGSSDPRET PMARTERRTL AVVASVGLTL ALATGALAAR
     GLSDDEEALA PTRGRPSAGI ERKVDALLAR MTTKEKLQQV QLLSDGQITD ADAKAGVGSV
     FSLVDAEKIN HFQRVAVEQS RLGIPILFAY DTVHGYRTVF PVPLGAASSF DPEVASADAE
     VGARESAIQG IKQVYSPMVD VSHEPRWGRI VEGAGEDPYL GSVMGAARVK GAQGTDYSRP
     DKVVSSVKHY VAYGEAEGGR DYNTTDLSES RLRNLYLPPF KAAIDAGADT VMCSFNSING
     VPGCANKYTE TDILKKEWGF DGFIESDYTA VAELRACPPV TPDEGPCGHG VAADGPQAGA
     AALMAGTDSE MVSTNIRDYG EQLLASRQIT MKRLDDAVRR ILRVKFRAGL FDHPYVDVAK
     ASDPASYGKP ADLAKSRWAA GRSMVLLKND GGALPLDPAR STALIGPFGD TVDDVLGPWP
     GRGADELAPA HVPLVEGLTA ASTGQVTYTQ ACNLAHNFDP PNVANPPLTP EDEVCAGPGD
     DGTTIDDAVA AAEAADQVVL ALGENAYMSG EANARSELTL PGQQQKLLDA VAATGKPVVV
     VLLNGRPLDL SAVQGKAAAI FEAWFPGTEG GHAVADVLFG TVNPGGKLPV TFPRRVGTAP
     TYYNHEPTGR PCDAASKYNS RYRDLATCDP LYPFGFGLSY TTFEVGDLRL SRSSVRRDGR
     LTASMRVTNT GSVAGDEVAQ LYLHDPVASL SQPVRRLRGF QRVSLDPGQS TTVTFTLDAS
     DFGFYDNRGK YVVEPGLIEV YGGDSSTATM KATFTVTR
//
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