ID   GUN1_BACIU              Reviewed;         499 AA.
AC   P07983;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   24-JAN-2024, entry version 115.
DE   RecName: Full=Endoglucanase;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=bglC; Synonyms=gld;
OS   Bacillus subtilis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DLG;
RX   PubMed=3106328; DOI=10.1128/jb.169.5.2017-2025.1987;
RA   Robson L.M., Chambliss G.H.;
RT   "Endo-beta-1,4-glucanase gene of Bacillus subtilis DLG.";
RL   J. Bacteriol. 169:2017-2025(1987).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA22496.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M16185; AAA22496.1; ALT_INIT; Genomic_DNA.
DR   PIR; A26874; A26874.
DR   AlphaFoldDB; P07983; -.
DR   SMR; P07983; -.
DR   STRING; 483913.AN935_09445; -.
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; Endoglucanase-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 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   PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 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_0000007839"
FT   DOMAIN          350..499
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   REGION          330..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  55187 MW;  339D04EE95A63EE1 CRC64;
     MKRSISIFIT CLLIAVLTMG GLLPSPASAA GTKTPVAKNG QLSIKGTQLV NRDGKAVQLK
     GISSHGLQWY GDFVNKDSLK WLRDDWGITV FRAAMYTADG GYIDNPSVKN KVKEAVEAAK
     ELGIYVIIDW HILNDGNPNQ NKEKAKEFFK EMSSLYGNTP NVIYEIANEP NGDVNWKRDI
     KPYAEEVISV IRKNDPDNII IVGTGTWSQD VNDAADDQLK DANVMYALHF YAGTHGQSLR
     DKANYALSKG APIFVTEWGT SDASGNGGVF LDQSREWLNY LDSKNISWVN WNLSDKQESS
     SALKPGASKT GGWPLTDLTA SGTFVRENIR GTKDSTKDVP ETPAQDNPTQ EKGVSVQYKA
     GDGRVNSNQI RPQLHIKNNG NATVDLKDVT ARYWYNVKNK GQNFDCDYAQ MGCGNLTHKF
     VTLHKPKQGA DTYLELGFKT GTLSPGASTG NIQLRLHNDD WSNYAQSGDY SFFQSNTFKT
     TKKITLYHQG KLIWGTEPN
//