P10475 (GUN2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase
EC=3.2.1.4

Alternative name(s):
Carboxymethyl-cellulase
Short name=CMCase
Short name=Cellulase
Endo-1,4-beta-glucanase

Gene names

Name:	eglS
Synonyms:	bglC, gld
Ordered Locus Names:	BSU18130

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	499 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	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. Contains 1 CBM3 (carbohydrate binding type-3) domain.
Sequence caution	The sequence CAA97610.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cellulase activity Inferred from electronic annotation. Source: EC cellulose binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Ref.5

Chain

30 – 499

470

Endoglucanase

PRO_0000007840

Regions

Domain

350 – 499

150

CBM3

Sites

Active site

169

1

Proton donor By similarity

Active site

257

1

Nucleophile By similarity

Experimental info

Sequence conflict

283

1

S → N in CAA47429. Ref.2

Secondary structure

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499

Helix Strand Turn

Details...

Helix

36 – 39

4

Beta strand

43 – 45

3

Beta strand

48 – 50

3

Beta strand

60 – 65

6

Helix

67 – 70

4

Helix

71 – 73

3

Helix

76 – 85

10

Beta strand

89 – 98

10

Turn

102 – 104

3

Helix

106 – 108

3

Helix

109 – 122

14

Beta strand

125 – 131

7

Beta strand

133 – 135

3

Turn

138 – 141

4

Helix

142 – 156

15

Beta strand

162 – 165

4

Turn

176 – 179

4

Helix

180 – 194

15

Beta strand

196 – 198

3

Beta strand

200 – 202

3

Helix

205 – 208

4

Helix

211 – 215

5

Beta strand

224 – 231

8

Turn

232 – 234

3

Helix

237 – 248

12

Beta strand

253 – 261

9

Helix

271 – 283

13

Beta strand

288 – 294

7

Helix

315 – 317

3

Helix

320 – 330

11

Beta strand

355 – 360

6

Beta strand

373 – 377

5

Helix

386 – 388

3

Beta strand

389 – 395

7

Beta strand

403 – 409

7

Beta strand

417 – 422

6

Beta strand

427 – 429

3

Beta strand

432 – 438

7

Beta strand

447 – 450

4

Beta strand

452 – 457

6

Turn

466 – 473

8

Beta strand

484 – 488

5

Beta strand

491 – 494

4

Sequences

	Sequence		Length	Mass (Da)
	P10475 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 8F735FF711B3EAE2	FASTA	499	55,287
	10 20 30 40 50 60 MKRSISIFIT CLLITLLTMG GMIASPASAA GTKTPVAKNG QLSIKGTQLV NRDGKAVQLK 70 80 90 100 110 120 GISSHGLQWY GEYVNKDSLK WLRDDWGITV FRAAMYTADG GYIDNPSVKN KVKEAVEAAK 130 140 150 160 170 180 ELGIYVIIDW HILNDGNPNQ NKEKAKEFFK EMSSLYGNTP NVIYEIANEP NGDVNWKRDI 190 200 210 220 230 240 KPYAEEVISV IRKNDPDNII IVGTGTWSQD VNDAADDQLK DANVMYALHF YAGTHGQFLR 250 260 270 280 290 300 DKANYALSKG APIFVTEWGT SDASGNGGVF LDQSREWLKY LDSKTISWVN WNLSDKQESS 310 320 330 340 350 360 SALKPGASKT GGWRLSDLSA SGTFVRENIL GTKDSTKDIP ETPSKDKPTQ ENGISVQYRA 370 380 390 400 410 420 GDGSMNSNQI RPQLQIKNNG NTTVDLKDVT ARYWYKAKNK GQNFDCDYAQ IGCGNVTHKF 430 440 450 460 470 480 VTLHKPKQGA DTYLELGFKN GTLAPGASTG NIQLRLHNDD WSNYAQSGDY SFFKSNTFKT 490 TKKITLYDQG KLIWGTEPN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of a Bacillus subtilis endo-beta-1,4-glucanase gene." Mackay R.M., Lo A., Willick G., Zuker M., Baird S., Dove M., Moranelli F., Seligy V. Nucleic Acids Res. 14:9159-9170(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PAP115.
[2]	"Nucleotide sequence of an endo-beta-1,4-glucanase gene from Bacillus subtilis CK-2." Lindahl V., Aa K., Tronsmo A. Antonie Van Leeuwenhoek 66:327-332(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CK-2.
[3]	"New genes in the 170 degrees region of the Bacillus subtilis genome encode DNA gyrase subunits, a thioredoxin, a xylanase and an amino acid transporter." Rose M., Entian K.-D. Microbiology 142:3097-3101(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[4]	"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.
[5]	"Characterization of production and enzyme properties of an endo-beta-1,4-glucanase from Bacillus subtilis CK-2 isolated from compost soil." Aa K., Flengsrud R., Lindahl V., Tronsmo A. Antonie Van Leeuwenhoek 66:319-326(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-45. Strain: CK-2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z29076 Genomic DNA. Translation: CAA82317.1.
X04689 Genomic DNA. Translation: CAA28392.1.
X67044 Genomic DNA. Translation: CAA47429.1.
Z73234 Genomic DNA. Translation: CAA97610.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB13696.2.

PIR

G69593.

RefSeq

NP_389695.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2L8A	NMR	-	A	354-499	[»]
3PZT	X-ray	1.97	A/B	27-332	[»]
3PZU	X-ray	2.10	A/B	27-332	[»]
3PZV	X-ray	2.87	A/B/C/D	27-332	[»]

ProteinModelPortal

P10475.

SMR

P10475. Positions 36-329, 353-498.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU18130.

Protein family/group databases

CAZy

CBM3. Carbohydrate-Binding Module Family 3.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB13696; CAB13696; BSU18130.

GeneID

938607.

KEGG

bsu:BSU18130.

PATRIC

18975461. VBIBacSub10457_1922.

Organism-specific databases

GenoList

BSU18130. [Micado]

Phylogenomic databases

HOGENOM

HOG000253566.

KO

K01179.

OMA

IIDWHIL.

ProtClustDB

CLSK927926.

Enzyme and pathway databases

BioCyc

BSUB:BSU18130-MONOMER.

Family and domain databases

Gene3D

2.60.40.710. 1 hit.
3.20.20.80. 1 hit.

InterPro

IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF00942. CBM_3. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]

SMART

SM01067. CBM_3. 1 hit.
[Graphical view]

SUPFAM

SSF49384. Cellul_bind. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS51172. CBM3. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P10475.

Entry information

Entry name

GUN2_BACSU

Accession

Primary (citable) accession number: P10475

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program