ID E3FTP1_STIAD Unreviewed; 1080 AA.
AC E3FTP1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN Name=celA {ECO:0000313|EMBL:ADO69655.1};
GN OrderedLocusNames=STAUR_1851 {ECO:0000313|EMBL:ADO69655.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO69655.1, ECO:0000313|Proteomes:UP000001351};
RN [1] {ECO:0000313|EMBL:ADO69655.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO69655.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
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; CP002271; ADO69655.1; -; Genomic_DNA.
DR RefSeq; WP_013374905.1; NC_014623.1.
DR AlphaFoldDB; E3FTP1; -.
DR STRING; 378806.STAUR_1851; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR KEGG; sur:STAUR_1851; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_9_1_7; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000001351; 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; 2.60.120.430; Galactose-binding lectin; 1.
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 InterPro; IPR041443; Exop_C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 PANTHER; PTHR30620:SF77; BETA-GLUCOSIDASE BOGH3B-LIKE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF18559; Exop_C; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1080
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003169727"
FT DOMAIN 79..420
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 458..674
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
FT DOMAIN 737..881
FT /note="ExoP galactose-binding-like"
FT /evidence="ECO:0000259|Pfam:PF18559"
FT REGION 679..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1080 AA; 115008 MW; E41FF10C2968ED8E CRC64;
MKRPAVWWKF SSSAALALLW LGACHPEDAG EPASSLPEPS EEATPLMGTA AVAWPKVQSA
IAVDAALEAK VEALLASMTL EEKVGQMMQV EIGNVTPAEI KQYHLGSVLN GGGSFPGGRK
NASVQDWVML ADQLWDASMD PSKARRIPII WGTDAVHGHN NVRGATFFPH NIGLGAANDP
ELIRRIGEVT AREVARTGVD WAFAPTIAVV RDDRWGRTYE GYSEDPAVVE AYAGKAVQGF
QGLLGKDAKS SEKVIATAKH FLGDGGTTRG VDQGVTSVTE QDLRDIHGKG YFTALAAGSQ
TVMASFNSWQ DTALGTNAKA LKMHGNKYLL TEVLKNQMGF DGFVVSDWNG HGQVKRSNSD
SAIDCTNGNC PQAINAGIDM VMVPYRDDWK ALITNTLASV RNGQIPESRI NDAVRRILRV
KYRAGLFEKP KPSLRNTSRE VGSAEHRAVA REAVRKSLVL LKNNGGTLPL SRSAKILVAG
KSANSLQNQN GGWSLTWQGT GNSNADFGGG VTAWQAIQKI VPSATLDTST NGALADSSYA
AAVVVIGETP YAEGVGDLSS TTLELAKLRP EDLALIDSLK AKGVKKIVTV LFSGRPLYAN
KEINRSDAFV AAWLPGTEGD GLADVLFRNA AGAVNYDFTG KLSYSWPKSP CQVQVNRGNA
GYAPLYAYGY GLTYASGQEQ GQHAETTQSG DCGDSGDGGG GGGTTSLVMF NRGNQNGWVM
RVGAPSNWDG IAVAQSTSTA TSTAGNELSA TPVDDRNGLQ WAAVKATWNN ATAEIYMQNS
NKTEVKNLQT YLSSGGALVF DARVSTKPSG AVKARVDCVY PCAGEIDITN ALNALPVNSW
TELAIPLQCF AAKGTDFTRI NTSVLLYSQG ALELSLANIR WEPSRAANVS CEGNLGAPGQ
LFADKDVYVN GVYDTALFSG PNVWKSGSGS VTLSPAFNTG TETVIDVVYT NLTEGGGNGV
VSLPVKDPLF LDVSQIAATG GVQFDIKVLS YGGTTQNFWT KIVCDRNPNQ CATGDLKTLI
GRPAVGTWKT VKVPFTSSSY PSTWKNDKLS SAVEVLPAWD DQRGTIRFQL RNIRILKQLN
//
