GUN1_BACIU
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 03-AUG-2022, entry version 111.
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; Firmicutes; 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 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_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