Reviewed, UniProtKB/Swiss-Prot P23550 (GUNB_PAELA)

Names and origin

Protein names

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

Gene names

Name:

celB

Organism

Paenibacillus lautus (Bacillus lautus)

Taxonomic identifier

1401 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Paenibacillaceae › Paenibacillus

Protein attributes

Sequence length	566 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.

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	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 – 30	30
	Chain	31 – 566	536	Endoglucanase B		PRO_0000007835
Sites
	Active site	177	1	Proton donor By similarity
	Active site	299	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	P23550-1 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 6426C8D8E29022C9	FASTA	566	62,622
	10 20 30 40 50 60 MKKRRSSKVI LSLAIVVALL AAVEPNAALA AAPPSAMQSY VEAMQPGWNL GNSLDAVGAD 70 80 90 100 110 120 ETLARGNPRI TKELIQNIAA QGYKSIRIPV TWDSHIGAAP NYQIEAAYLN RVQEVVQWAL 130 140 150 160 170 180 DANLYVMINV HHDSWLWISK MESQHDQVLA RYNAIWTQIA NKFKNSPSKL MFESVNEPRF 190 200 210 220 230 240 TDGGTTDEAK QQKMLDELNV SFFNIVRNSG GQNATRPLVL STLEASPTQE RMTALYNTMT 250 260 270 280 290 300 KLNDKNLIAT VHFYGFWPFS VNIAGYTKFD AETQNDIITT FDNVYNTFVA KGIPVVVGEY 310 320 330 340 350 360 GLLGFDKNTG VIEQGEKLKF FEFFAQYVKQ KSISTMLWDN GQHFNRTSFK WSDPDLFNMI 370 380 390 400 410 420 KASWTGRSST ASSDLIHVKQ GTAVKDTSVQ LNLNGNTLTS LSVNGTTLKS GTDYTLNSSR 430 440 450 460 470 480 LTFKASQLTK LTSLGKLGVN ATIVTKFNRG ADWKFNVVLY NTPKLSSTTG TTSSFAIPTA 490 500 510 520 530 540 FNGDQLATME AVYVNGGNAG PHNWTSFKEF ETTFSPAYSE GKIKLQQAFF NEVNDTTVTL 550 560 KFQFWSGEIV NYTIKKSGST VTGTAS

References

[1]	"Multiple endo-beta-1,4-glucanase-encoding genes from Bacillus lautus PL236 and characterization of the celB gene." Joergensen P.L., Hansen C.K. Gene 93:55-60(1990) [PubMed: 2227426] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PL236.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M33762 Genomic DNA. Translation: AAA22408.1.
PIR	JH0218.
3D structure databases
HSSP	HSSP built from PDB template 1EDG based on UniProtKB P17901.
ModBase	Search...
Protein family/group databases
CAZy	CBM46. Carbohydrate-Binding Module Family 46. GH5. Glycoside Hydrolase Family 5.
Enzyme and pathway databases
BRENDA	3.2.1.4. 297505.
Family and domain databases
InterPro	IPR005102. DUF291. IPR001547. Glyco_hydro_5. IPR018087. Glyco_hydro_5_CS. IPR016282. Glyco_hydro_5_endoGlcnase_B. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00150. Cellulase. 1 hit. PF03442. DUF291. 1 hit. [Graphical view]
PIRSF	PIRSF001043. Endoglucanase_B. 1 hit.
PROSITE	PS00659. GLYCOSYL_HYDROL_F5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUNB_PAELA

Accession

Primary (citable) accession number: P23550

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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