Reviewed, UniProtKB/Swiss-Prot P06565 (GUN2_BACS4)

Names and origin

Protein names

Recommended name:
    Endoglucanase B
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase B
    Cellulase B

Gene names

Name:

celB

Organism

Bacillus sp. (strain N-4 / JCM 9156)

Taxonomic identifier

1413 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro cellulase 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

Chain

1 – 409

409

Endoglucanase B

PRO_0000184045

Sites

Active site

165

1

Proton donor By similarity

Active site

254

1

Nucleophile By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

409

Helix Strand Turn

Details...

Helix

31 – 35

5

Beta strand

39 – 41

3

Beta strand

44 – 46

3

Beta strand

56 – 61

6

Helix

63 – 66

4

Helix

67 – 69

3

Helix

72 – 80

9

Beta strand

85 – 94

10

Turn

98 – 100

3

Helix

102 – 104

3

Helix

105 – 118

14

Beta strand

121 – 127

7

Beta strand

129 – 131

3

Helix

134 – 137

4

Helix

138 – 152

15

Beta strand

158 – 161

4

Turn

173 – 176

4

Helix

177 – 189

13

Beta strand

193 – 195

3

Beta strand

197 – 199

3

Helix

202 – 205

4

Helix

208 – 212

5

Beta strand

221 – 228

8

Helix

234 – 245

12

Beta strand

250 – 258

9

Helix

268 – 280

13

Beta strand

285 – 291

7

Helix

312 – 314

3

Helix

317 – 328

12

Sequences

	Sequence		Length	Mass (Da)
	P06565-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 9888660E66B4DA3F	FASTA	409	45,690
	10 20 30 40 50 60 MKKITTIFVV LLMTLALFII GNTTAADDYS VVEEHGQLSI SNGELVNDRG EPVQLKGMSS 70 80 90 100 110 120 HGLQWYGQFV NYESMKWLRD DWGITVFRAA MYTSSGGYIE DPSVKEKVKE AVEAAIDLGI 130 140 150 160 170 180 YVIIDWHILS DNDPNIYKEE AKDFFDEMSE LYGDYPNVIY EIANEPNGSD VTWDNQIKPY 190 200 210 220 230 240 AEEVIPVIRN NDPNNIIIVG TGTWSQDVHH AADNQLTDPN VMYAFHFYAG THGQNLRDQV 250 260 270 280 290 300 DYALDQGAAI FVSEWGTSEA TGDGGVFLDE AQVWIDFMDE RNLSWANWSL THKDESSAAL 310 320 330 340 350 360 MPGASPTGGW TEAELSPSGT FVREKIRESA TTPPSDPTPP SDPDPGEPEP DPGEPDPTPP 370 380 390 400 SDPGDYPAWD PNTIYTDEIV YHNGQLWQAK WWTQNQEPGD PYGPWEPLN

References

[1]	"Nucleotide sequences of two cellulase genes from alkalophilic Bacillus sp. strain N-4 and their strong homology." Fukumori F., Sashihara N., Kudo T., Horikoshi K. J. Bacteriol. 168:479-485(1986) [PubMed: 3782013] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14729 Genomic DNA. Translation: AAA22299.1.

PIR

B25156.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E5J	X-ray	1.85	A	30-330	[»]
1QHZ	X-ray	1.95	A	30-330	[»]
1QI0	X-ray	2.10	A	30-330	[»]
1QI2	X-ray	1.75	A	30-330	[»]
4A3H	X-ray	1.65	A	30-329	[»]
8A3H	X-ray	0.97	A	30-329	[»]

SMR

P06565. Positions 363-407.

ModBase

Search...

Protein family/group databases

CAZy

CBM5. Carbohydrate-Binding Module Family 5.
GH5. Glycoside Hydrolase Family 5.

Family and domain databases

InterPro

IPR003610. Carb-bd_dom_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR017853. Glyco_hydro_catalytic_core.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF02839. CBM_5_12. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]

SMART

SM00495. ChtBD3. 1 hit.
[Graphical view]

PROSITE

PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUN2_BACS4

Accession

Primary (citable) accession number: P06565

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	January 19, 2010
This is version 73 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)