P28622 (GUN4_BACS5) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Endoglucanase 4 EC=3.2.1.4 Alternative name(s): Cellulase 4 EG-IV Endo-1,4-beta-glucanase 4
Organism	Bacillus sp. (strain KSM-522)
Taxonomic identifier	120046 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	636 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.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 9 (cellulase E) family. Contains 1 CBM3 (carbohydrate binding type-3) domain.
Caution	Was originally (Ref.2) thought to originate from Clostridium cellulovorans and was termed endoglucanase C (engC).

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 cellulose 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 – 25	25	Potential
	Chain	26 – 636	611	Endoglucanase 4		PRO_0000007952
Regions
	Domain	478 – 635	158	CBM3
Sites
	Active site	400	1	By similarity
	Active site	438	1	By similarity
	Active site	447	1	By similarity
Experimental info
	Sequence conflict	530 – 534	5	AKGFT → CEGIH Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P28622 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 76718BF57A8EF6A2	FASTA	636	72,245
	10 20 30 40 50 60 MTRRWSFLVQ CFTFKKKEGV RSRYMSDYNY VEVLQKSILF YEAQRSGKLP ESNRLNWRGD 70 80 90 100 110 120 SGLEDGKDVG HDLTGGWYDA GDHVKFGLPM AYSAAVLAWT VYEYREAYEE AELLDDMLDQ 130 140 150 160 170 180 IKWATDYFLK AHTGPNEFWA QVGDGNADHG WWGPAEVMPM NRPAFKIDEH CPGTEVAAQT 190 200 210 220 230 240 AAALAAGSII FKETDAPYAA KLLTHAKQLY AFADQYRGEY TDCVTNAQPF YNSWSGYIDE 250 260 270 280 290 300 LIWGGIWLYL ATNDQTYLNK ALKAVEEWPK DWDYTFTMSW DNTFFLSQIL LARITKEKRF 310 320 330 340 350 360 IESTERNLDY WSTGFVQNGK VERITYTPGG LAWLDQWGSL RYTANAAFLA FVYADWVSDQ 370 380 390 400 410 420 EKKNRYQTFA IRQTHYMLGD NPQNRSYVVG FGKNPPMHPH HRTAHGSWSN QLTTPSSHRH 430 440 450 460 470 480 TLYGPLVGGP NRQDQYTDDI SDYVSNEVAT DYNAAFTGNG AAVWSGQSKL PNFPPKEKVE 490 500 510 520 530 540 DEFFVEAAVM SNDTTSTQIK AILYNRSGWP ARSSQSLSFR YYVNLSEIFA KGFTDKDIQV 550 560 570 580 590 600 TAVYNEGASL SPLTVYDASS HIYFTEIDFT GVAIFPGGES LHKKEIQFRL SAPNGANIWD 610 620 630 ASNDYSFQGL TSNMQKTARI PVFDQGDLVF GTLPNK

References

[1]	"Amino acid sequence and stereoselective hydrolytic reaction of an endo-1,4-beta-glucanase from a Bacillus strain." Hitomi J., Hatada Y., Kawaminami S., Kawai S., Ito S. Biosci. Biotechnol. Biochem. 61:2004-2009(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning of Clostridium cellulovorans endo-1,4-beta-glucanase genes." Shoseyov O., Foong F., Hamamoto T., Doi R.H. Biochem. Biophys. Res. Commun. 169:667-672(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-534.
[3]	Doi R.H. Unpublished observations (JAN-2000) Cited for: SHOWS THAT SEQUENCE DID NOT ORIGINATE FROM C.CELLULOVORANS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB004098 Genomic DNA. Translation: BAA24918.1.
PIR	JC5874.
3D structure databases
ProteinModelPortal	P28622.
SMR	P28622. Positions 27-634.
ModBase	Search...
Protein family/group databases
CAZy	CBM3. Carbohydrate-Binding Module Family 3. GH9. Glycoside Hydrolase Family 9.
Proteomic databases
PRIDE	P28622.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.50.10.10. 1 hit. 2.60.40.710. 1 hit.
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR012341. 6hp_glycosidase. IPR008965. Carb-bd_dom. IPR001956. CBD_3. IPR001701. Glyco_hydro_9. IPR018221. Glyco_hydro_9_AS. [Graphical view]
Pfam	PF00942. CBM_3. 1 hit. PF00759. Glyco_hydro_9. 1 hit. [Graphical view]
SMART	SM01067. CBM_3. 1 hit. [Graphical view]
SUPFAM	SSF49384. Cellul_bind. 1 hit. SSF48208. Glyco_trans_6hp. 1 hit.
PROSITE	PS51172. CBM3. 1 hit. PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit. PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUN4_BACS5

Accession

Primary (citable) accession number: P28622
Secondary accession number(s): O50589

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	May 30, 2000
Last modified:	April 3, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program