ID   GUNB_CLOC7              Reviewed;         440 AA.
AC   P28621; D9SUK1;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Endoglucanase B;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase B;
DE   AltName: Full=Endo-1,4-beta-glucanase B;
DE   AltName: Full=Endo-1,4-beta-xylanase;
DE            EC=3.2.1.8;
DE   Flags: Precursor;
GN   Name=engB; OrderedLocusNames=Clocel_1150;
OS   Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=573061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1955860; DOI=10.1099/00221287-137-7-1729;
RA   Foong F., Hamamoto T., Shoseyov O., Doi R.H.;
RT   "Nucleotide sequence and characteristics of endoglucanase gene engB from
RT   Clostridium cellulovorans.";
RL   J. Gen. Microbiol. 137:1729-1736(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Hemme C.L., Woyke T.;
RT   "Complete sequence of Clostridium cellulovorans 743B.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has endoglucanase activity on carboxymethyl-cellulose (CMC),
CC       xylan and lichenan, but not Avicel.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- MISCELLANEOUS: Up to 32 AA of the N-terminus and 52 AA of the C-
CC       terminus are not required for catalytic activity.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; M75706; AAA23231.1; -; Genomic_DNA.
DR   EMBL; CP002160; ADL50906.1; -; Genomic_DNA.
DR   PIR; A44815; A44815.
DR   RefSeq; WP_010076241.1; NC_014393.1.
DR   AlphaFoldDB; P28621; -.
DR   SMR; P28621; -.
DR   IntAct; P28621; 1.
DR   STRING; 573061.Clocel_1150; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   EnsemblBacteria; ADL50906; ADL50906; Clocel_1150.
DR   KEGG; ccb:Clocel_1150; -.
DR   eggNOG; COG2730; Bacteria.
DR   HOGENOM; CLU_018668_3_1_9; -.
DR   OMA; HYYDPWD; -.
DR   OrthoDB; 1395441at2; -.
DR   Proteomes; UP000002730; Chromosome.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1330.10; -; 1.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF63446; SSF63446; 1.
DR   PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..440
FT                   /note="Endoglucanase B"
FT                   /id="PRO_0000007847"
FT   DOMAIN          381..440
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT   ACT_SITE        179
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        305
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   440 AA;  48637 MW;  93D6CB9EA7E2AF21 CRC64;
     MNKRLSRGKI SLLASVFVTT TFMGGVNVLA STAKTGIRDI TSQQVVKEMK VGWNLGNTMD
     ATGGETNWGN PLTTHAMIDK VKAAGFNTLR LPITWDGHIG AAPDYAIDAT WMNRVEEIAN
     YAFDNNMYVI INLHHEDGWL KPYYANEAEV KAKITKVWTQ IANRFKDYGD YLIFETMNEP
     RPVGAADEWS GGSYENRDMV NRYNLTAVNT IRATGGNNAL RHIMVPTLAA AALSTTMNDY
     IVPNNDSRVI VSLHMYSPYF FSADLTSQWT TATWGSDADK AALSADFDAV YNKFVKNGRA
     VVIGEMGTIN KNNLDSRVKH AEYYAKEATV RGITPIWWDN GYCVAGKEQT FGIFNRKNLT
     WCCPEVMQAF IRGAGATQTQ TSYSLGDVNK DGKVNAIDYA VLKSILLGTN TNVDLSVSDM
     NKDGKVNALD LAVLKKMLLS