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Database: UniProt
Entry: W7CPL1_9LIST
LinkDB: W7CPL1_9LIST
Original site: W7CPL1_9LIST 
ID   W7CPL1_9LIST            Unreviewed;       921 AA.
AC   W7CPL1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:EUJ41584.1};
GN   ORFNames=BCAMP_03345 {ECO:0000313|EMBL:EUJ41584.1};
OS   Brochothrix campestris FSL F6-1037.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX   NCBI_TaxID=1265861 {ECO:0000313|EMBL:EUJ41584.1, ECO:0000313|Proteomes:UP000019243};
RN   [1] {ECO:0000313|EMBL:EUJ41584.1, ECO:0000313|Proteomes:UP000019243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL F6-1037 {ECO:0000313|EMBL:EUJ41584.1,
RC   ECO:0000313|Proteomes:UP000019243};
RA   den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A.,
RA   Nightingale K.K., Kephart D., Wiedmann M.;
RT   "Novel taxa of Listeriaceae from agricultural environments in the United
RT   States.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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:EUJ41584.1}.
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DR   EMBL; AODH01000011; EUJ41584.1; -; Genomic_DNA.
DR   RefSeq; WP_051456844.1; NZ_AODH01000011.1.
DR   AlphaFoldDB; W7CPL1; -.
DR   STRING; 1265861.BCAMP_03345; -.
DR   PATRIC; fig|1265861.3.peg.653; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000019243; 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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019243};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        91..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          462..536
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   921 AA;  101818 MW;  75E0649356DC35DD CRC64;
     MSGKLTKRRS RKIKMSEQLT RDRAERQARR LAIKQLPLAQ KKEALVADKR AQKRARLNDK
     RVLKALPKAE RNERKKEAKV YRKLKNRPRR LIIWSAVALV VVGVAIKIGP TAAHMYTIMS
     GKNVVINTET PAGEKARALG NKVSREIAAE GIVLMKNEAD NLPLKDTRVN VFGTAAFNFR
     YGGGGSGGID TSAAVNLFDG LKQADVSYNQ ELRQFYEALP EVKKAEATQN DSGMMQVVKS
     MISGNDEDEP AIAYLKEKVI KQAQAYSDNA VILLASSGVE SSDMSQEQLQ LTKNKRALIQ
     TVAANFDNVT VVVNAGNALE LGYLEEFPQI KSIVWVGTPG PYGTAALGDV LAGKVNPSGR
     LTDTYAYDAK SAPATENFGD YKYNNLKQSY VNYQEGIYIG YRYYETYYKD DEVGYHKAVQ
     FPYGHGLSYT DFDWEIVDKQ LTTDKITVEV AVTNTGKRAG KDVVQLYYSA PYTNGGLEKS
     AVVLGAFGKT KLLQPGEKQT LTLSYSTNDM ASYDANKEEA YVLEAGDYQL KLAQNVHQST
     LDFTYKVPKT KVIKTDAVTG TTIKNQFAAS EADLTYLSRA DWQGTYPSDK ANNHRAPQFV
     LDELAKKPTD SKLPMPQFEQ DNQLKLADLK GLAYDDPKWE QFLDQFTKEE LIDYVVNGAY
     QTEAIDRLGV PSAMLLDGPA GLNSFFKKFK AASFPSENVL AATWNDQLGY AMGAAIGKEA
     KVYGVHGWYA PAVNLHRTSM GGRNFEYFSE DPVLSGKMGA AVIKGAQAQD IIVFMKHFAM
     NDQETNARSG LYVWANEQSI RELHLRPFEI AVKEGKTLGT MSSFSLINGK WTGGNAELLN
     QVLRDEWGFE GVVSSDAVFG FMHADDAVVS GNDLMLDTMS APKNVKRIKA AYEADPSGTA
     IGLRTSVHNI MYALLQTYLI K
//
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