Reviewed, UniProtKB/Swiss-Prot P27051 (GUB_BACLI)

Names and origin

Protein names

Recommended name:
    Beta-glucanase
    EC=3.2.1.73
Alternative name(s):
    Endo-beta-1,3-1,4 glucanase
    1,3-1,4-beta-D-glucan 4-glucanohydrolase
    Lichenase

Gene names

Name:

bg1

Organism

Bacillus licheniformis

Taxonomic identifier

1402 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	243 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
Miscellaneous	Beta-glucanases of Bacillus have a substrate range similar to lichenase of germinating barley.
Sequence similarities	Belongs to the glycosyl hydrolase 16 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	licheninase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Potential

Chain

28 – 243

216

Beta-glucanase

PRO_0000011788

Sites

Active site

134

1

Nucleophile

Active site

138

1

Proton donor

Amino acid modifications

Disulfide bond

61 ↔ 90

Ref.5

Experimental info

Mutagenesis

51

1

D → N: 30% of wild-type activity.

Mutagenesis

89

1

D → N: 85% of wild-type activity.

Mutagenesis

92

1

E → Q: 3% of wild-type activity.

Mutagenesis

105

1

E → Q: 50% of wild-type activity.

Mutagenesis

133

1

D → N: 15% of wild-type activity.

Mutagenesis

134

1

E → Q: 0.2% of wild-type activity.

Mutagenesis

136

1

D → N: 0.5% of wild-type activity.

Mutagenesis

138

1

E → Q: Complete loss of activity.

Mutagenesis

143

1

D → N: 65% of wild-type activity.

Mutagenesis

160

1

E → Q: 15% of wild-type activity.

Mutagenesis

168

1

D → N: 60% of wild-type activity.

Mutagenesis

179

1

D → N: 80% of wild-type activity.

Mutagenesis

190

1

D → N: 70% of wild-type activity.

Mutagenesis

219

1

D → N: No change in activity.

Sequence conflict

232

1

S → Y Ref.5

Secondary structure

1

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243

Helix Strand Turn

Details...

Beta strand

35 – 37

3

Turn

44 – 46

3

Beta strand

47 – 49

3

Beta strand

61 – 63

3

Helix

65 – 67

3

Beta strand

68 – 70

3

Beta strand

76 – 84

9

Beta strand

87 – 97

11

Beta strand

101 – 109

9

Beta strand

116 – 124

9

Helix

126 – 128

3

Beta strand

133 – 140

8

Beta strand

146 – 153

8

Beta strand

161 – 164

4

Turn

169 – 171

3

Beta strand

174 – 181

8

Beta strand

184 – 189

6

Beta strand

192 – 197

6

Beta strand

206 – 217

12

Helix

219 – 222

4

Beta strand

231 – 242

12

Sequences

	Sequence		Length	Mass (Da)
	P27051-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 651188D9AAD609A5	FASTA	243	27,435
	10 20 30 40 50 60 MSYRVKRMLM LLVTGLFLSL STFAASASAQ TGGSFYEPFN NYNTGLWQKA DGYSNGNMFN 70 80 90 100 110 120 CTWRANNVSM TSLGEMRLSL TSPSYNKFDC GENRSVQTYG YGLYEVNMKP AKNVGIVSSF 130 140 150 160 170 180 FTYTGPTDGT PWDEIDIEFL GKDTTKVQFN YYTNGVGNHE KIVNLGFDAA NSYHTYAFDW 190 200 210 220 230 240 QPNSIKWYVD GQLKHTATTQ IPQTPGKIMM NLWNGAGVDE WLGSYNGVTP LSRSLHWVRY TKR

References

[1]	"Molecular cloning, expression and nucleotide sequence of the endo-beta-1,3-1,4-D-glucanase gene from Bacillus licheniformis. Predictive structural analyses of the encoded polypeptide." Lloberas J., Perez-Pons J.A., Querol E. Eur. J. Biochem. 197:337-343(1991) [PubMed: 2026156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Querol E. Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Essential catalytic role of Glu134 in endo-beta-1,3-1,4-D-glucan 4-glucanohydrolase from B. licheniformis as determined by site-directed mutagenesis." Planas A., Juncosa M., Lloberas J., Querol E. FEBS Lett. 308:141-145(1992) [PubMed: 1354172] [Abstract] Cited for: MUTAGENESIS.
[4]	"Identification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase by site-directed mutagenesis." Juncosa M., Pons J., Dot T., Querol E., Planas A. J. Biol. Chem. 269:14530-14535(1994) [PubMed: 8182059] [Abstract] Cited for: MUTAGENESIS.
[5]	"Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8-A resolution." Hahn M., Pons J., Planas A., Querol E., Heinemann U. FEBS Lett. 374:221-224(1995) [PubMed: 7589539] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), DISULFIDE BOND.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X57279 Genomic DNA. Translation: CAA40547.1.

PIR

S15388.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GBG	X-ray	1.80	A	30-243	[»]
3D6E	X-ray	2.40	A/B	30-243	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH16. Glycoside Hydrolase Family 16.

Enzyme and pathway databases

BRENDA

3.2.1.73. 1017.

Family and domain databases

InterPro

IPR008264. Beta_glucanase.
IPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
[Graphical view]

Gene3D

G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.

Pfam

PF00722. Glyco_hydro_16. 1 hit.
[Graphical view]

PRINTS

PR00737. GLHYDRLASE16.

PROSITE

PS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUB_BACLI

Accession

Primary (citable) accession number: P27051

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	November 24, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)