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Protein

Beta-glucanase

Gene

bglS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei133 – 1331NucleophilePROSITE-ProRule annotation
Active sitei137 – 1371Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. licheninase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciBSUB:BSU39070-MONOMER.

Protein family/group databases

CAZyiGH16. Glycoside Hydrolase Family 16.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucanase (EC:3.2.1.73)
Alternative name(s):
1,3-1,4-beta-D-glucan 4-glucanohydrolase
Endo-beta-1,3-1,4 glucanase
Lichenase
Gene namesi
Name:bglS
Synonyms:bgl, licS
Ordered Locus Names:BSU39070
ORF Names:N15B
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU39070. [Micado]

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28281 PublicationAdd
BLAST
Chaini29 – 242214Beta-glucanasePRO_0000011791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291Pyrrolidone carboxylic acid
Disulfide bondi60 ↔ 89By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP04957.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU39070.

Structurei

Secondary structure

1
242
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 363Combined sources
Turni43 – 453Combined sources
Beta strandi46 – 483Combined sources
Beta strandi60 – 623Combined sources
Helixi64 – 663Combined sources
Beta strandi67 – 693Combined sources
Beta strandi75 – 839Combined sources
Beta strandi86 – 9611Combined sources
Beta strandi100 – 1089Combined sources
Beta strandi115 – 1239Combined sources
Helixi125 – 1273Combined sources
Beta strandi132 – 1398Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi160 – 1634Combined sources
Helixi168 – 1703Combined sources
Beta strandi173 – 1797Combined sources
Beta strandi184 – 1885Combined sources
Beta strandi191 – 1966Combined sources
Beta strandi205 – 21612Combined sources
Helixi218 – 2214Combined sources
Beta strandi230 – 24112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3O5SX-ray2.20A29-242[»]
ProteinModelPortaliP04957.
SMRiP04957. Positions 29-242.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04957.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 16 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2273.
HOGENOMiHOG000250723.
InParanoidiP04957.
OMAiNGSHQNC.
OrthoDBiEOG6JB18P.
PhylomeDBiP04957.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008264. Beta_glucanase.
IPR013320. ConA-like_dom.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
[Graphical view]
PfamiPF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
PRINTSiPR00737. GLHYDRLASE16.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04957-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPYLKRVLLL LVTGLFMSLF AVTATASAQT GGSFFDPFNG YNSGFWQKAD
60 70 80 90 100
GYSNGNMFNC TWRANNVSMT SLGEMRLALT SPAYNKFDCG ENRSVQTYGY
110 120 130 140 150
GLYEVRMKPA KNTGIVSSFF TYTGPTDGTP WDEIDIEFLG KDTTKVQFNY
160 170 180 190 200
YTNGAGNHEK IVDLGFDAAN AYHTYAFDWQ PNSIKWYVDG QLKHTATNQI
210 220 230 240
PTTPGKIMMN LWNGTGVDEW LGSYNGVNPL YAHYDWVRYT KK
Length:242
Mass (Da):27,269
Last modified:November 1, 1995 - v2
Checksum:i45958DEA70F22B29
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241A → S in strain: HL-25.
Natural varianti83 – 831A → S in strain: HL-25.
Natural varianti204 – 2041P → L in strain: C120.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00754 Genomic DNA. Translation: CAA25328.1.
D00518 Genomic DNA. Translation: BAA00405.1.
D83026 Genomic DNA. Translation: BAA11697.1.
Z46862 Genomic DNA. Translation: CAA86922.1.
AL009126 Genomic DNA. Translation: CAB15943.1.
Z28340 Genomic DNA. Translation: CAA82195.1.
PIRiI40370. LXBS.
RefSeqiNP_391786.1. NC_000964.3.
WP_003244531.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15943; CAB15943; BSU39070.
GeneIDi937470.
KEGGibsu:BSU39070.
PATRICi18979872. VBIBacSub10457_4098.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00754 Genomic DNA. Translation: CAA25328.1.
D00518 Genomic DNA. Translation: BAA00405.1.
D83026 Genomic DNA. Translation: BAA11697.1.
Z46862 Genomic DNA. Translation: CAA86922.1.
AL009126 Genomic DNA. Translation: CAB15943.1.
Z28340 Genomic DNA. Translation: CAA82195.1.
PIRiI40370. LXBS.
RefSeqiNP_391786.1. NC_000964.3.
WP_003244531.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3O5SX-ray2.20A29-242[»]
ProteinModelPortaliP04957.
SMRiP04957. Positions 29-242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU39070.

Protein family/group databases

CAZyiGH16. Glycoside Hydrolase Family 16.

Proteomic databases

PaxDbiP04957.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15943; CAB15943; BSU39070.
GeneIDi937470.
KEGGibsu:BSU39070.
PATRICi18979872. VBIBacSub10457_4098.

Organism-specific databases

GenoListiBSU39070. [Micado]

Phylogenomic databases

eggNOGiCOG2273.
HOGENOMiHOG000250723.
InParanoidiP04957.
OMAiNGSHQNC.
OrthoDBiEOG6JB18P.
PhylomeDBiP04957.

Enzyme and pathway databases

BioCyciBSUB:BSU39070-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP04957.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008264. Beta_glucanase.
IPR013320. ConA-like_dom.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
[Graphical view]
PfamiPF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
PRINTSiPR00737. GLHYDRLASE16.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of the gene and genetic control sites for the excreted B. subtilis enzyme beta-glucanase."
    Murphy N., McConnell D.J., Cantwell B.A.
    Nucleic Acids Res. 12:5355-5367(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C120.
  2. "Construction of a beta-glucanase hyperproducing Bacillus subtilis using the cloned beta-glucanase gene and a multi-copy plasmid."
    Tezuka H., Yuuki T., Yabuuchi S.
    Agric. Biol. Chem. 53:2335-2339(1989)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: HL-25.
  3. "Sequencing of a 65 kb region of the Bacillus subtilis genome containing the lic and cel loci, and creation of a 177 kb contig covering the gnt-sacXY region."
    Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y., Fujita Y.
    Microbiology 142:3113-3123(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / BGSC1A1.
  4. "Genes encoding xylan and beta-glucan hydrolysing enzymes in Bacillus subtilis: characterization, mapping and construction of strains deficient in lichenase, cellulase and xylanase."
    Wolf M., Geczi A., Simon O., Borriss R.
    Microbiology 141:281-290(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  5. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  6. "LicT, a Bacillus subtilis transcriptional antiterminator protein of the BglG family."
    Schnetz K., Stuelke J., Gertz S., Krueger S., Krieg M., Hecker M., Rak B.
    J. Bacteriol. 178:1971-1979(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
    Strain: 168 / BR151.
  7. "Purification and some properties of two enzymes from a beta-glucanase hyperproducing strain, Bacillus subtilis HL-25."
    Yuuki T., Tezuka H., Yabuuchi S.
    Agric. Biol. Chem. 53:2341-2346(1989)
    Cited for: PROTEIN SEQUENCE OF 29-63.

Entry informationi

Entry nameiGUB_BACSU
AccessioniPrimary (citable) accession number: P04957
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Beta-glucanases of Bacillus have a substrate range similar to lichenase of germinating barley.
The sequence of strain 168 is shown.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.