GUB_BACSU
ID GUB_BACSU Reviewed; 242 AA.
AC P04957;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 148.
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=bglS; Synonyms=bgl, licS; OrderedLocusNames=BSU39070; ORFNames=N15B;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C120;
RX PubMed=6087283; DOI=10.1093/nar/12.13.5355;
RA Murphy N., McConnell D.J., Cantwell B.A.;
RT "The DNA sequence of the gene and genetic control sites for the excreted B.
RT subtilis enzyme beta-glucanase.";
RL Nucleic Acids Res. 12:5355-5367(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HL-25;
RA Tezuka H., Yuuki T., Yabuuchi S.;
RT "Construction of a beta-glucanase hyperproducing Bacillus subtilis using
RT the cloned beta-glucanase gene and a multi-copy plasmid.";
RL Agric. Biol. Chem. 53:2335-2339(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=8969509; DOI=10.1099/13500872-142-11-3113;
RA Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y.,
RA Fujita Y.;
RT "Sequencing of a 65 kb region of the Bacillus subtilis genome containing
RT the lic and cel loci, and creation of a 177 kb contig covering the gnt-
RT sacXY region.";
RL Microbiology 142:3113-3123(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7704256; DOI=10.1099/13500872-141-2-281;
RA Wolf M., Geczi A., Simon O., Borriss R.;
RT "Genes encoding xylan and beta-glucan hydrolysing enzymes in Bacillus
RT subtilis: characterization, mapping and construction of strains deficient
RT in lichenase, cellulase and xylanase.";
RL Microbiology 141:281-290(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RC STRAIN=168 / BR151;
RX PubMed=8606172; DOI=10.1128/jb.178.7.1971-1979.1996;
RA Schnetz K., Stuelke J., Gertz S., Krueger S., Krieg M., Hecker M., Rak B.;
RT "LicT, a Bacillus subtilis transcriptional antiterminator protein of the
RT BglG family.";
RL J. Bacteriol. 178:1971-1979(1996).
RN [7]
RP PROTEIN SEQUENCE OF 29-63, AND PYROGLUTAMATE FORMATION AT GLN-29.
RA Yuuki T., Tezuka H., Yabuuchi S.;
RT "Purification and some properties of two enzymes from a beta-glucanase
RT hyperproducing strain, Bacillus subtilis HL-25.";
RL Agric. Biol. Chem. 53:2341-2346(1989).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: Beta-glucanases of Bacillus have a substrate range
CC similar to lichenase of germinating barley.
CC -!- MISCELLANEOUS: The sequence of strain 168 is shown.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR EMBL; X00754; CAA25328.1; -; Genomic_DNA.
DR EMBL; D00518; BAA00405.1; -; Genomic_DNA.
DR EMBL; D83026; BAA11697.1; -; Genomic_DNA.
DR EMBL; Z46862; CAA86922.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15943.1; -; Genomic_DNA.
DR EMBL; Z28340; CAA82195.1; -; Genomic_DNA.
DR PIR; I40370; LXBS.
DR RefSeq; NP_391786.1; NC_000964.3.
DR RefSeq; WP_003244531.1; NZ_JNCM01000034.1.
DR PDB; 3O5S; X-ray; 2.20 A; A=29-242.
DR PDBsum; 3O5S; -.
DR AlphaFoldDB; P04957; -.
DR SMR; P04957; -.
DR STRING; 224308.BSU39070; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; P04957; -.
DR PRIDE; P04957; -.
DR EnsemblBacteria; CAB15943; CAB15943; BSU_39070.
DR GeneID; 937470; -.
DR KEGG; bsu:BSU39070; -.
DR PATRIC; fig|224308.179.peg.4230; -.
DR eggNOG; COG2273; Bacteria.
DR InParanoid; P04957; -.
DR OMA; WYVSDGW; -.
DR PhylomeDB; P04957; -.
DR BioCyc; BSUB:BSU39070-MON; -.
DR BRENDA; 3.2.1.73; 658.
DR SABIO-RK; P04957; -.
DR EvolutionaryTrace; P04957; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 3D-structure; Direct protein sequencing; Disulfide bond; Glycosidase;
KW Hydrolase; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|Ref.7"
FT CHAIN 29..242
FT /note="Beta-glucanase"
FT /id="PRO_0000011791"
FT DOMAIN 29..242
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 133
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 137
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT MOD_RES 29
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.7"
FT DISULFID 60..89
FT /evidence="ECO:0000250"
FT VARIANT 24
FT /note="A -> S (in strain: HL-25)"
FT VARIANT 83
FT /note="A -> S (in strain: HL-25)"
FT VARIANT 204
FT /note="P -> L (in strain: C120)"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3O5S"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3O5S"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:3O5S"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:3O5S"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 205..216
FT /evidence="ECO:0007829|PDB:3O5S"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:3O5S"
FT STRAND 230..241
FT /evidence="ECO:0007829|PDB:3O5S"
SQ SEQUENCE 242 AA; 27269 MW; 45958DEA70F22B29 CRC64;
MPYLKRVLLL LVTGLFMSLF AVTATASAQT GGSFFDPFNG YNSGFWQKAD GYSNGNMFNC
TWRANNVSMT SLGEMRLALT SPAYNKFDCG ENRSVQTYGY GLYEVRMKPA KNTGIVSSFF
TYTGPTDGTP WDEIDIEFLG KDTTKVQFNY YTNGAGNHEK IVDLGFDAAN AYHTYAFDWQ
PNSIKWYVDG QLKHTATNQI PTTPGKIMMN LWNGTGVDEW LGSYNGVNPL YAHYDWVRYT
KK
