ID   GUB_BREBE               Reviewed;         259 AA.
AC   P37073;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Beta-glucanase;
DE            EC=3.2.1.73;
DE   AltName: Full=1,3-1,4-beta-D-glucan 4-glucanohydrolase;
DE   AltName: Full=Endo-beta-1,3-1,4 glucanase;
DE   AltName: Full=Lichenase;
DE   Flags: Precursor;
GN   Name=bglBB;
OS   Brevibacillus brevis (Bacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Alk36;
RX   PubMed=7763386; DOI=10.1007/bf00242946;
RA   Louw M.E., Reid S.J., Watson T.G.;
RT   "Characterization, cloning and sequencing of a thermostable endo-(1,3-1,4)
RT   beta-glucanase-encoding gene from an alkalophilic Bacillus brevis.";
RL   Appl. Microbiol. Biotechnol. 38:507-513(1993).
CC   -!- FUNCTION: Hydrolyzes B-glucans containing mixed beta-1,3 and beta-1,4
CC       linkages.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-
CC         glucans containing (1->3)- and (1->4)-bonds.; EC=3.2.1.73;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 65-70 degrees Celsius. Thermostable.;
CC   -!- MISCELLANEOUS: Beta-glucanases of Bacillus have a substrate range
CC       similar to lichenase of germinating barley.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR   EMBL; M84339; AAA22265.1; -; Genomic_DNA.
DR   PIR; A48378; A48378.
DR   AlphaFoldDB; P37073; -.
DR   SMR; P37073; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   BRENDA; 3.2.1.73; 638.
DR   GO; GO:0042972; F:licheninase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR044791; Beta-glucanase/XTH.
DR   InterPro; IPR008264; Beta_glucanase.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR008263; GH16_AS.
DR   PANTHER; PTHR31062; PTHR31062; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   PRINTS; PR00737; GLHYDRLASE16.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS01034; GH16_1; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..259
FT                   /note="Beta-glucanase"
FT                   /id="PRO_0000011787"
FT   DOMAIN          35..255
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        142
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   ACT_SITE        146
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
SQ   SEQUENCE   259 AA;  29960 MW;  A63C09F281FF5D13 CRC64;
     MVKSKYLVFI SVFSLLFGVF VVGFSHQGVK AEEERPMGTA FYESFDAFDD ERWSKAGVWT
     NGQMFNATWY PEQVTADGLM RLTIAKKTTS ARNYKAGELR TNDFYHYGLF EVSMKPAKVE
     GTVSSFFTYT GEWDWDGDPW DEIDIEFLGK DTTRIQFNYF TNGVGGNEFY YDLGFDASES
     FNTYAFEWRE DSITWYVNGE AVHTATENIP QTPQKIMMNL WPGVGVDGWT GVFDGDNTPV
     YSYYDWVRYT PLQNYQIHQ