ID   GUNB_ACET2              Reviewed;         563 AA.
AC   P04956; A3DCU3;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 135.
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            Short=EgB;
DE   Flags: Precursor;
GN   Name=celB; OrderedLocusNames=Cthe_0536;
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=203119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3453102; DOI=10.1093/nar/14.4.1791;
RA   Grepinet O., Beguin P.;
RT   "Sequence of the cellulase gene of Clostridium thermocellum coding for
RT   endoglucanase B.";
RL   Nucleic Acids Res. 14:1791-1799(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC   B-4536 / VPI 7372;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA   Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme catalyzes the endohydrolysis of 1,4-beta-
CC       glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; X03592; CAA27266.1; -; Genomic_DNA.
DR   EMBL; CP000568; ABN51772.1; -; Genomic_DNA.
DR   PIR; A23512; CZCLBM.
DR   RefSeq; WP_003517581.1; NC_009012.1.
DR   AlphaFoldDB; P04956; -.
DR   SMR; P04956; -.
DR   STRING; 203119.Cthe_0536; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   DNASU; 4808285; -.
DR   EnsemblBacteria; ABN51772; ABN51772; Cthe_0536.
DR   KEGG; cth:Cthe_0536; -.
DR   eggNOG; COG2730; Bacteria.
DR   eggNOG; COG4447; Bacteria.
DR   HOGENOM; CLU_020735_2_0_9; -.
DR   OMA; ETDNMGH; -.
DR   OrthoDB; 1395441at2; -.
DR   BioCyc; MetaCyc:MON-16415; -.
DR   BRENDA; 3.2.1.4; 1530.
DR   Proteomes; UP000002145; Chromosome.
DR   GO; GO:0008810; F:cellulase 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; 1.
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..27
FT                   /note="Or 31"
FT   CHAIN           28..563
FT                   /note="Endoglucanase B"
FT                   /id="PRO_0000007850"
FT   DOMAIN          496..562
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT   REGION          476..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        204
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        363
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   563 AA;  63929 MW;  866FE55704A1DE4B CRC64;
     MKKFLVLLIA LIMIATLLVV PGVQTSAEGS YADLAEPDDD WLHVEGTNIV DKYGNKVWIT
     GANWFGFNCR ERMLLDSYHS DIIADIELVA DKGINVVRMP IATDLLYAWS QGIYPPSTDT
     SYNNPALAGL NSYELFNFML ENFKRVGIKV ILDVHSPETD NQGHNYPLWY NTTITEEIFK
     KAWVWVAERY KNDDTIIGFD LKNEPHTNTG TMKIKAQSAI WDDSNHPNNW KRVAEETALA
     ILEVHPNVLI FVEGVEMYPK DGIWDDETFD TSPWTGNNDY YGNWWGGNLR GVKDYPINLG
     KYQSQLVYSP HDYGPIVYEQ DWFKGDFITA NDEQAKRILY EQCWRDNWAY IMEEGISPLL
     LGEWGGMTEG GHPLLDLNLK YLRCMRDFIL ENKYKLHHTF WCINIDSADT GGLFTRDEGT
     PFPGGRDLKW NDNKYDNYLY PVLWKTEDGK FIGLDHKIPL GRNGISISQL SNYTPSVTPS
     PSATPSPTTI TAPPTDTVTY GDVNGDGRVN SSDVALLKRY LLGLVENINK EAADVNVSGT
     VNSTDLAIMK RYVLRSISEL PYK