Reviewed, UniProtKB/Swiss-Prot P07983 (GUN1_BACSU)

Names and origin

Protein names

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

Gene names

Name:	bglC
Synonyms:	gld

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
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
	Signal peptide	1 – 29	29
	Chain	30 – 499	470	Endoglucanase		PRO_0000007839
Regions
	Domain	350 – 499	150	CBM3
Sites
	Active site	169	1	Proton donor By similarity
	Active site	257	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	P07983-1 [UniParc]. Last modified November 1, 1991. Version 2. Checksum: 339D04EE95A63EE1	FASTA	499	55,187
	10 20 30 40 50 60 MKRSISIFIT CLLIAVLTMG GLLPSPASAA GTKTPVAKNG QLSIKGTQLV NRDGKAVQLK 70 80 90 100 110 120 GISSHGLQWY GDFVNKDSLK 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 YAGTHGQSLR 250 260 270 280 290 300 DKANYALSKG APIFVTEWGT SDASGNGGVF LDQSREWLNY LDSKNISWVN WNLSDKQESS 310 320 330 340 350 360 SALKPGASKT GGWPLTDLTA SGTFVRENIR GTKDSTKDVP ETPAQDNPTQ EKGVSVQYKA 370 380 390 400 410 420 GDGRVNSNQI RPQLHIKNNG NATVDLKDVT ARYWYNVKNK GQNFDCDYAQ MGCGNLTHKF 430 440 450 460 470 480 VTLHKPKQGA DTYLELGFKT GTLSPGASTG NIQLRLHNDD WSNYAQSGDY SFFQSNTFKT 490 TKKITLYHQG KLIWGTEPN

References

[1]	"Endo-beta-1,4-glucanase gene of Bacillus subtilis DLG." Robson L.M., Chambliss G.H. J. Bacteriol. 169:2017-2025(1987) [PubMed: 3106328] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DLG.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M16185 Genomic DNA. Translation: AAA22496.1. Different initiation.
PIR	A26874.
3D structure databases
SMR	P07983. Positions 36-330, 351-498.
ModBase	Search...
Protein family/group databases
CAZy	CBM3. Carbohydrate-Binding Module Family 3. GH5. Glycoside Hydrolase Family 5.
Enzyme and pathway databases
BRENDA	3.2.1.4. 150.
Family and domain databases
InterPro	IPR008965. Carb_bd. IPR001956. CBD_3. IPR001547. Glyco_hydro_5. IPR018087. Glyco_hydro_5_CS. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.40.710. CBD_3. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00942. CBM_3. 1 hit. PF00150. Cellulase. 1 hit. [Graphical view]
PROSITE	PS51172. CBM3. 1 hit. PS00659. GLYCOSYL_HYDROL_F5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUN1_BACSU

Accession

Primary (citable) accession number: P07983

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	November 1, 1991
Last modified:	January 19, 2010
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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