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Database: UniProt
Entry: V6K5Q8_STRRC
LinkDB: V6K5Q8_STRRC
Original site: V6K5Q8_STRRC 
ID   V6K5Q8_STRRC            Unreviewed;       443 AA.
AC   V6K5Q8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN   ORFNames=M878_25665 {ECO:0000313|EMBL:EST27388.1};
OS   Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST27388.1, ECO:0000313|Proteomes:UP000017984};
RN   [1] {ECO:0000313|EMBL:EST27388.1, ECO:0000313|Proteomes:UP000017984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS 12.976 {ECO:0000313|EMBL:EST27388.1,
RC   ECO:0000313|Proteomes:UP000017984};
RX   PubMed=24407645;
RA   Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT   "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT   12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL   Genome Announc. 2:e01147-e01113(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6.
CC       {ECO:0000256|RuleBase:RU361186}.
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:EST27388.1}.
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DR   EMBL; AWQX01000214; EST27388.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6K5Q8; -.
DR   STRING; 1352936.M878_25665; -.
DR   PATRIC; fig|1352936.5.peg.5353; -.
DR   HOGENOM; CLU_556456_0_0_11; -.
DR   OrthoDB; 309899at2; -.
DR   Proteomes; UP000017984; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR016288; Beta_cellobiohydrolase.
DR   InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001524; Glyco_hydro_6_CS.
DR   PANTHER; PTHR34876; -; 1.
DR   PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF01341; Glyco_hydro_6; 1.
DR   PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR   PRINTS; PR00733; GLHYDRLASE6.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1.
DR   PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361186};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW   ECO:0000256|RuleBase:RU361186};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361186};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361186};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361186};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017984};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          7..130
FT                   /note="CBM-cenC"
FT                   /evidence="ECO:0000259|Pfam:PF02018"
FT   ACT_SITE        264
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10057"
FT   ACT_SITE        417
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         411
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
SQ   SEQUENCE   443 AA;  46139 MW;  F4D7A433F7B904B8 CRC64;
     MAALYGDLVT NGSFTDGVSG WWAGDPAMLA LNAPGAGLQA TATTEAVNLW DAPFGQDKIT
     LRAGCTYTLS FTARASQPGT QLRAQVGLGT DPWTAALDRT VTLPAVDTHF VLRFTSALDT
     TAGQVSFQFG QGTTVTIYLT EVRLTCSTVR EGFYADLESN AAKWVAANPD DPRARKIAHG
     LVRRPAARWF GNWNKDIKAD VDAYVAAAAA VGRLPILAAY NVHNRDAGGQ SSGGAFSPEE
     YRAWIDAFAE GIGDRPALVI VEPDSLAQLG NLSTDAARAE RTSLIAHAAE VLAALPLVHA
     YLDGGNATWI RPGDMAERLA AAGVAKVRGF AVGVANFDAT DISCTYGQQV STALSGLGVH
     GARFVIDTSR NGNGALDGNG QHAGYCNPAG RRLGVPSSMG IGGAEYLLWI KAPGDSDGLG
     GTAPTTAAGT FSPFLAEHLI DGR
//
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