O08342 (GUNA_PAEBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase A
EC=3.2.1.4

Alternative name(s):
Cellulase A
Endo-1,4-beta-D-glucanase A

Gene names

Name:

celA

Organism

Paenibacillus barcinonensis

Taxonomic identifier

198119 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Paenibacillus

Protein attributes

Sequence length	400 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	Endoglucanase with high activity on carboxymethylcellulose (CMC) and lichenan, but not active on Avicel. Ref.1
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Ref.1
Enzyme regulation	Strongly inhibited by Hg2+, Ag+ and Fe3+. To a lesser extent, is also inhibited by Pb2+, Mn2+, Sn2+ and Cu2+. By contrast, Ni2+, Zn2+, Co2+, Ba2+ and NH4+ do not affect enzyme activity, while 10 mM Ca2+, and Mg2+ produce a stimulating effect. Is also strongly inhibited by chemicals such as N-bromosuccinimide and dimethyl(2-dihydroxy-5-nitrobenzyl)sulphonium bromide. Is not affected by N-acetylimidazole. Ref.1
Subcellular location	Secreted Ref.1.
Biotechnological use	Study of the performance of endoglucanase A on paper manufacture from agricultural fibers shows that treatment with the enzyme improves the properties of the pulp and the quality of paper. CelA treatment enhances the physical properties (stretch and tensile index) of paper from wheat straw, while dewatering properties are slightly diminished. Ref.1
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Biophysicochemical properties	pH dependence: Optimum pH is 4.0. Highly stable at acid pH. Retains 100% of its activity after 90 minutes incubation at pH 4.5 and 45 degrees Celsius, and 95% of the initial activity is found after 15 days incubation at room temperature and pH 4.5. Ref.1 Temperature dependence: Optimum temperature is 40 degrees Celsius. Shows 98% and 51% of its maximum activity at 45 and 55 degrees Celsius, respectively.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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
	Signal peptide	1 – 32	32	Probable
	Chain	33 – 400	368	Endoglucanase A		PRO_0000371421
Sites
	Active site	187	1	Proton donor By similarity
	Active site	328	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	O08342 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: E89CB35BBC6F8AE5	FASTA	400	44,799
	10 20 30 40 50 60 MTKTFKKFSI AGLALLFMAT AAFAGWSTKA SAADMRSLTA AQITAEMGAG WNLGNQLEAT 70 80 90 100 110 120 VNGTPNETSW GNPTITPELI KKVKAAGFKT IRIPVSYLNY IGSAPNYTVN ASWLNRIQQV 130 140 150 160 170 180 VDYAYNEGLY VVINMHGDGF HSIPGSWLHV NSSNQNVIRD KYQKVWQQVA TRFSAYNERL 190 200 210 220 230 240 IFESMNEVFD GNYNNPNTSY YGNLNAYNQI FVDTVRKTGG NNNARWLLVP GWNTNIDYTV 250 260 270 280 290 300 GNYGFVVPTD NFRSSAIPSS QKRIMISAHY YSPWDFAGEE NGNITQWGAT ATNPAKRSTW 310 320 330 340 350 360 GQEDYLDSQF KSMYDKFVTQ GYPVVMGEFG SIDKSSYDSS NNNYRAVYAK AVTATAKKYK 370 380 390 400 LVPVYWDNGF NGQHGFALFN RFNNTVTQQN IINAIMQGMQ

References

[1]

"Cloning of a new endoglucanase gene from Bacillus sp. BP-23 and characterisation of the enzyme. Performance in paper manufacture from cereal straw." Blanco A., Diaz P., Martinez J., Vidal T., Torres A.L., Pastor F.I.J. Appl. Microbiol. Biotechnol. 50:48-54(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOTECHNOLOGY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. Strain: DSM 15478 / CECT 7022 / BP-23.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y12512 Genomic DNA. Translation: CAA73113.1.
3D structure databases
HSSP	HSSP built from PDB template 1EDG based on UniProtKB P17901.
ProteinModelPortal	O08342.
SMR	O08342. Positions 40-400.
ModBase	Search...
Protein family/group databases
CAZy	GH5. Glycoside Hydrolase Family 5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR001547. Glyco_hydro_5. IPR018087. Glyco_hydro_5_CS. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00150. Cellulase. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00659. GLYCOSYL_HYDROL_F5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUNA_PAEBA

Accession

Primary (citable) accession number: O08342

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program