ID   GUN_BACSZ               Reviewed;         463 AA.
AC   P29019;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Endoglucanase;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   AltName: Full=Endo-K;
DE   Flags: Precursor;
OS   Bacillus sp. (strain KSM-330).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=72575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1770347; DOI=10.1099/00221287-137-10-2299;
RA   Ozaki K., Sumitomo N., Ito S.;
RT   "Molecular cloning and nucleotide sequence of the gene encoding an endo-
RT   1,4-beta-glucanase from Bacillus sp. KSM-330.";
RL   J. Gen. Microbiol. 137:2299-2305(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 56-75, AND CHARACTERIZATION.
RX   PubMed=2045781; DOI=10.1099/00221287-137-1-41;
RA   Ozaki K., Ito S.;
RT   "Purification and properties of an acid endo-1,4-beta-glucanase from
RT   Bacillus sp. KSM-330.";
RL   J. Gen. Microbiol. 137:41-48(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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.2. Active from pH 4.5 to 6.5.;
CC   -!- PTM: The N- and the C-terminus may be subjected to proteolysis.
CC   -!- MISCELLANEOUS: One Trp residue has been proved to be involved in the
CC       mechanism of action of endo-K.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family.
CC       {ECO:0000305}.
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DR   EMBL; M68872; AAA22409.1; -; Genomic_DNA.
DR   PIR; A44808; A44808.
DR   AlphaFoldDB; P29019; -.
DR   SMR; P29019; -.
DR   CAZy; GH8; Glycoside Hydrolase Family 8.
DR   PRIDE; P29019; -.
DR   SABIO-RK; P29019; -.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR002037; Glyco_hydro_8.
DR   InterPro; IPR019834; Glyco_hydro_8_CS.
DR   Pfam; PF01270; Glyco_hydro_8; 1.
DR   PRINTS; PR00735; GLHYDRLASE8.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   PROSITE; PS00812; GLYCOSYL_HYDROL_F8; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..55
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007931"
FT   CHAIN           56..463
FT                   /note="Endoglucanase"
FT                   /id="PRO_0000007932"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        191
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10058"
SQ   SEQUENCE   463 AA;  51883 MW;  407FA54F5236C59E CRC64;
     MVEKRKIFTV LCACGIGFTS YTSCISAAAI DNDTLINNGH KINSSIITNS SQVSAVAKEM
     KPFPQQVNYS GILKPNHVSQ ESLNNAVKNY YNDWKKKYLK NDLSSLPGGY YVKGEITGNP
     DGFRPLGTSE GQGYGMIITV LMAGHDSNAQ TIYDGLFKTA RAFKSSINPN LMGWVVADDK
     KAQGHFDSAT DGDLDIAYSL LLAHKQWGSS GKINYLKEAQ NMITKGIKAS NVTKNNGLNL
     GDWGDKSTFD TRPSDWMMSH LRAFYEFTGD KTWLNVIDNL YNTYTNFTNK YSPKTGLISD
     FVVKNPPQPA PKDFLDESKY TDSYYYNASR VPLRIVMDYA MYGEKRGKVI SDKVATWIKS
     KTKGNPSKIV DGYKLDGTNI GDYPTAVYVS PFIAAGTTNS KNQEWVNSGW DWMKNKKESY
     FSDSYNLLTM LFLTGNWWKP IPDEKKIQSP INLEVQSELK EQD