ID   GUB_PAEPO               Reviewed;         238 AA.
AC   P45797;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=gluB;
OS   Paenibacillus polymyxa (Bacillus polymyxa).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 842 / DSM 36 / JCM 2507 / NBRC 15309 / NCIMB 8158 / NCTC 10343
RC   / NRRL B-4317 / VKM B-514;
RX   PubMed=1938968; DOI=10.1128/jb.173.23.7705-7710.1991;
RA   Gosalbes M.J., Perez-Gonzalez J.A., Gonzalez R., Navarro A.;
RT   "Two beta-glycanase genes are clustered in Bacillus polymyxa: molecular
RT   cloning, expression, and sequence analysis of genes encoding a xylanase and
RT   an endo-beta-(1,3)-(1,4)-glucanase.";
RL   J. Bacteriol. 173:7705-7710(1991).
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   -!- 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; X57094; CAA40379.1; -; Genomic_DNA.
DR   PIR; S19012; S19012.
DR   AlphaFoldDB; P45797; -.
DR   SMR; P45797; -.
DR   STRING; 1052684.PPM_2346; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   eggNOG; COG2273; Bacteria.
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   3: Inferred from homology;
KW   Disulfide bond; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..238
FT                   /note="Beta-glucanase"
FT                   /id="PRO_0000011790"
FT   DOMAIN          29..238
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        129
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   DISULFID        56..85
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   238 AA;  26919 MW;  C0CF7B4EA5D40E8C CRC64;
     MMKKKSWFTL MITGVISLFF SVSAFAGNVF WEPLSYFNSS TWQKADGYSN GQMFNCTWRA
     NNVNFTNDGK LKLSLTSPAN NKFDCGEYRS TNNYGYGLYE VSMKPAKNTG IVSSFFTYTG
     PSHGTQWDEI DIEFLGKDTT KVQFNYYTNG VGGHEKIINL GFDASTSFHT YAFDWQPGYI
     KWYVDGVLKH TATTNIPSTP GKIMMNLWNG TGVDSWLGSY NGANPLYAEY DWVKYTSN