P37651 (GUN_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase
EC=3.2.1.4

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

Gene names

Name:	bcsZ
Synonyms:	bcsC, yhjM
Ordered Locus Names:	b3531, JW3499

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	368 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)

Function	Hydrolyzes carboxymethylcellulose.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Pathway	Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular location	Secreted.
Miscellaneous	The genes bscA, bcsB, bcsZ and bcsC are constitutively transcribed but cellulose synthesis occurs only when AdrA, a putative transmembrane protein regulated by AgfD, is expressed. Cellulose production is abolished in E.coli K12.
Sequence similarities	Belongs to the glycosyl hydrolase 8 (cellulase D) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from direct assay Ref.1. Source: EcoCyc
Molecular_function	cellulase activity Inferred from direct assay Ref.1. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 368

347

Endoglucanase

PRO_0000007938

Sites

Active site

55

1

Proton donor By similarity

Active site

116

1

Nucleophile Potential

Secondary structure

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368

Helix Strand Turn

Details...

Helix

26 – 35

10

Beta strand

51 – 53

3

Helix

54 – 66

13

Helix

70 – 84

15

Turn

89 – 91

3

Beta strand

96 – 100

5

Beta strand

106 – 110

5

Helix

115 – 131

17

Helix

135 – 152

18

Beta strand

153 – 156

4

Turn

157 – 159

3

Beta strand

160 – 163

4

Beta strand

165 – 172

8

Beta strand

175 – 178

4

Helix

185 – 191

7

Helix

192 – 194

3

Helix

198 – 211

14

Beta strand

220 – 225

6

Turn

226 – 228

3

Beta strand

239 – 241

3

Turn

242 – 244

3

Helix

245 – 252

8

Helix

259 – 267

9

Helix

269 – 278

10

Beta strand

283 – 286

4

Turn

287 – 289

3

Beta strand

292 – 294

3

Helix

298 – 307

10

Helix

311 – 323

13

Helix

331 – 344

14

Beta strand

347 – 350

4

Beta strand

356 – 358

3

Sequences

	Sequence		Length	Mass (Da)
	P37651 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 6539C03D4D0CFDEA	FASTA	368	41,700
	10 20 30 40 50 60 MNVLRSGIVT MLLLAAFSVQ AACTWPAWEQ FKKDYISQEG RVIDPSDARK ITTSEGQSYG 70 80 90 100 110 120 MFSALAANDR AAFDNILDWT QNNLAQGSLK ERLPAWLWGK KENSKWEVLD SNSASDGDVW 130 140 150 160 170 180 MAWSLLEAGR LWKEQRYTDI GSALLKRIAR EEVVTVPGLG SMLLPGKVGF AEDNSWRFNP 190 200 210 220 230 240 SYLPPTLAQY FTRFGAPWTT LRETNQRLLL ETAPKGFSPD WVRYEKDKGW QLKAEKTLIS 250 260 270 280 290 300 SYDAIRVYMW VGMMPDSDPQ KARMLNRFKP MATFTEKNGY PPEKVDVATG KAQGKGPVGF 310 320 330 340 350 360 SAAMLPFLQN RDAQAVQRQR VADNFPGSDA YYNYVLTLFG QGWDQHRFRF STKGELLPDW GQECANSH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the Escherichia coli endo-1,4-D-glucanase gene and identification of its product." Park Y.W., Yun H.D. Mol. Gen. Genet. 261:236-241(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The multicellular morphotypes of Salmonella typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix." Zogaj X., Nimtz M., Rohde M., Bokranz W., Roemling U. Mol. Microbiol. 39:1452-1463(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: ECOR 10, ECOR 12 and TOB1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00039 Genomic DNA. Translation: AAB18508.1.
U00096 Genomic DNA. Translation: AAC76556.1.
AP009048 Genomic DNA. Translation: BAE77763.1.

PIR

S47752.

RefSeq

NP_417988.1. NC_000913.2.
YP_491904.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QXF	X-ray	1.85	A/B/C/D	22-368	[»]
3QXQ	X-ray	2.20	A/B/C/D	22-368	[»]

ProteinModelPortal

P37651.

SMR

P37651. Positions 24-360.

ModBase

Search...

Protein-protein interaction databases

IntAct

P37651. 3 interactions.

STRING

511145.b3531.

Protein family/group databases

CAZy

GH8. Glycoside Hydrolase Family 8.

Proteomic databases

PaxDb

P37651.

PRIDE

P37651.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76556; AAC76556; b3531.
BAE77763; BAE77763; BAE77763.

GeneID

12934278.
948046.

KEGG

ecj:Y75_p3646.
eco:b3531.

PATRIC

32122528. VBIEscCol129921_3642.

Organism-specific databases

EchoBASE

EB2167.

EcoGene

EG12258. bcsZ.

Phylogenomic databases

eggNOG

COG3405.

HOGENOM

HOG000259088.

KO

K01179.

OMA

IRVYLWV.

ProtClustDB

PRK11097.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12258-MONOMER.
ECOL316407:JW3499-MONOMER.
MetaCyc:EG12258-MONOMER.

UniPathway

UPA00694.

Gene expression databases

Genevestigator

P37651.

Family and domain databases

Gene3D

1.50.10.10. 1 hit.

InterPro

IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR002037. Glyco_hydro_8.
IPR019834. Glyco_hydro_8_CS.
[Graphical view]

Pfam

PF01270. Glyco_hydro_8. 1 hit.
[Graphical view]

PRINTS

PR00735. GLHYDRLASE8.

SUPFAM

SSF48208. Glyco_trans_6hp. 1 hit.

PROSITE

PS00812. GLYCOSYL_HYDROL_F8. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUN_ECOLI

Accession

Primary (citable) accession number: P37651
Secondary accession number(s): Q2M7J3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program