ID   GUN3_BACIU              Reviewed;         499 AA.
AC   P23549;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Endoglucanase;
DE            EC=3.2.1.4;
DE   AltName: Full=Carboxymethyl-cellulase;
DE            Short=CMCase;
DE            Short=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=bglC;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BSE616;
RX   PubMed=1368694; DOI=10.1271/bbb1961.55.441;
RA   Park S.H., Kim H.K., Pack M.Y.;
RT   "Characterization and structure of the cellulase gene of Bacillus subtilis
RT   BSE616.";
RL   Agric. Biol. Chem. 55:441-448(1991).
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; D01057; BAA00859.1; -; Genomic_DNA.
DR   PIR; JN0111; JN0111.
DR   AlphaFoldDB; P23549; -.
DR   BMRB; P23549; -.
DR   SMR; P23549; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.710; -; 1.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51172; CBM3; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..29
FT   CHAIN           30..499
FT                   /note="Endoglucanase"
FT                   /id="PRO_0000007841"
FT   DOMAIN          350..499
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   ACT_SITE        169
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   ACT_SITE        257
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         69..70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         263..264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         291
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         296..298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
SQ   SEQUENCE   499 AA;  55169 MW;  2E821E3D8BBACA04 CRC64;
     MKRSISIFIT CLLITLLTMG GMLASPASAA GTKTPVAKNG QLSIKGTQLV NRDGKAVQLK
     GISSHGLQWY GEYVNKDSLK WLRDDWGITV FRAAMYTADG GIIDNPSVKN KMKEAVEAAK
     ELGIYVIIDW HILNDGNPNQ NKEKAKEFFK EMSSLYGNTP NVIYEIANEP NGDVNWKRDI
     KPYAEEVISV IRKNDPDNII IVGTGTWSQD VNDAADDQLK DANVMDALHF YAGTHGQFLR
     DKANYALSKG APIFVTEWGT SDASGNGGVF LDQSREWLKY LDSKTISWVN WNLSDKQESS
     SALKPGASKT GGWRLSDLSA SGTFVRENIL GTKDSTKDIP ETPAKDKPTQ ENGISVQYRA
     GDGSMNSNQI RPQLQIKNNG NTTVDLKDVT ARYWYNAKNK GQNVDCDYAQ LGCGNVTYKF
     VTLHKPKQGA DTYLELGFKN GTLAPGASTG NIQLRLHNDD WSNYAQSGDY SFFKSNTFKT
     TKKITLYDQG KLIWGTEPN