P18126 (GUNB_CELJU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase B
Short name=EGB
EC=3.2.1.4

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

Gene names

Name:	celB
Synonyms:	cel45A
Ordered Locus Names:	CJA_0374

Organism

Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) [Complete proteome] [HAMAP]

Taxonomic identifier

498211 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Cellvibrio

Protein attributes

Sequence length	511 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	This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. EGB is most active against barley beta-glucan, but showed significant activity against amorphous and crystalline cellulose.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the glycosyl hydrolase 45 (cellulase K) family. Contains 1 CBM2 (carbohydrate binding type-2) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Periplasm
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cellulase activity Inferred from electronic annotation. Source: EC polysaccharide 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.1
	Chain	30 – 511	482	Endoglucanase B		PRO_0000008023
Regions
	Domain	30 – 130	101	CBM2
	Compositional bias	132 – 173	42	Ser-rich (linker)
	Compositional bias	223 – 259	37	Ser-rich
Sites
	Active site	276	1	Nucleophile By similarity
	Active site	393	1	Proton donor By similarity
Amino acid modifications
	Disulfide bond	32 ↔ 127		By similarity
	Disulfide bond	181 ↔ 212		By similarity
	Disulfide bond	191 ↔ 206		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P18126 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 3C3119D998291D8E	FASTA	511	52,078
	10 20 30 40 50 60 MNLLSGWVRP LMLGCGLLGA ALSAGSIQAA VCEYRVTNEW GSGFTASIRI TNNGSSTING 70 80 90 100 110 120 WSVSWNYTDG SRVTSSWNAG LSGANPYSAT PVGWNTSIPI GSSVEFGVQG NNGSSRAQVP 130 140 150 160 170 180 AVTGAICGGQ GSSAPSSVAS SSSSSSVVSS TPRSSSSSVS SSVPGTSSSS SSSVLTGAQA 190 200 210 220 230 240 CNWYGTLTPL CNNTSNGWGY EDGRSCVART TCSAQPAPYG IVSTSSSTPL SSSSSSRSSV 250 260 270 280 290 300 ASSSSLSSAT SSSASSVSSV PPIDGGCNGY ATRYWDCCKP HCGWSANVPS LVSPLQSCSA 310 320 330 340 350 360 NNTRLSDVSV GSSCDGGGGY MCWDKIPFAV SPTLAYGYAA TSSGDVCGRC YQLQFTGSSY 370 380 390 400 410 420 NAPGDPGSAA LAGKTMIVQA TNIGYDVSGG QFDILVPGGG VGAFNACSAQ WGVSNAELGA 430 440 450 460 470 480 QYGGFLAACK QQLGYNASLS QYKSCVLNRC DSVFGSRGLT QLQQGCTWFA EWFEAADNPS 490 500 510 LKYKEVPCPA ELTTRSGMNR SILNDIRNTC P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The N-terminal region of an endoglucanase from Pseudomonas fluorescens subspecies cellulosa constitutes a cellulose-binding domain that is distinct from the catalytic centre." Gilbert H.J., Hall J., Hazlewood G.P., Ferreira L.M.A. Mol. Microbiol. 4:759-767(1990) [PubMed: 2117693] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-48.
[2]	"Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus." DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E. J. Bacteriol. 190:5455-5463(2008) [PubMed: 18556790] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ueda107.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X52615 Genomic DNA. Translation: CAA36844.1. CP000934 Genomic DNA. Translation: ACE82688.1.
PIR	S10527.
RefSeq	YP_001980898.1. NC_010995.1.
3D structure databases
ProteinModelPortal	P18126.
SMR	P18126. Positions 177-224.
ModBase	Search...
Protein family/group databases
CAZy	CBM10. Carbohydrate-Binding Module Family 10. CBM2. Carbohydrate-Binding Module Family 2. GH45. Glycoside Hydrolase Family 45.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6416065.
GenomeReviews	Gene locus CJA_0374 in contig CP000934_GR.
KEGG	cja:CJA_0374.
PATRIC	21324125. VBICelJap122165_0383.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	QLGYNAS.
ProtClustDB	CLSK2544226.
Family and domain databases
InterPro	IPR014733. Barwin-like_endoglucanase. IPR009009. Barwin-related_endoglucanase. IPR008965. Carb-bd_dom. IPR012291. CBD_carb-bd_dom. IPR002883. CBM10/Dockerin_dom. IPR018366. CBM2_CS. IPR009031. CBM_fam10. IPR001919. Cellulose-bd_dom_fam2_bac. IPR000334. Glyco_hydro_45. [Graphical view]
Gene3D	G3DSA:2.40.40.10. Barwin. 1 hit. G3DSA:2.60.40.290. CBD_carb_bd. 1 hit. G3DSA:2.30.32.30. TypeX_cellulose-bd_reg_CBDX. 1 hit.
Pfam	PF02013. CBM_10. 1 hit. PF00553. CBM_2. 1 hit. PF02015. Glyco_hydro_45. 1 hit. [Graphical view]
SMART	SM00637. CBD_II. 1 hit. [Graphical view]
SUPFAM	SSF50685. Barwin_like. 1 hit. SSF57615. CBDX. 1 hit. SSF49384. Cellul_bind. 1 hit.
PROSITE	PS51173. CBM2. 1 hit. PS00561. CBM2_A. 1 hit. PS01140. GLYCOSYL_HYDROL_F45. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUNB_CELJU

Accession

Primary (citable) accession number: P18126
Secondary accession number(s): B3PI35

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program