Reviewed, UniProtKB/Swiss-Prot P22222 (E13B_CELCE)

Names and origin

Protein names	Recommended name:     Glucan endo-1,3-beta-glucosidase     EC=3.2.1.39 Alternative name(s):     (1->3)-beta-glucan endohydrolase       Short name=(1->3)-beta-glucanase
Organism	Cellulosimicrobium cellulans (Arthrobacter luteus)
Taxonomic identifier	1710 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Promicromonosporaceae › Cellulosimicrobium

Protein attributes

Sequence length	548 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	Lysis of cellular walls containing beta-1,3-glucans. Implicated in the defense against fungal pathogens.
Catalytic activity	Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Subcellular location	Periplasm. Ref.1
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Sequence similarities	Belongs to the glycosyl hydrolase 64 family. Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Periplasm
Domain	Signal
Ligand	Lectin
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glucan endo-1,3-beta-D-glucosidase activity Inferred from electronic annotation. Source: EC sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 36	36	Tat-type signal Ref.1
	Chain	37 – 548	512	Glucan endo-1,3-beta-glucosidase		PRO_0000012235
Regions
	Domain	422 – 548	127	Ricin B-type lectin
	Region	37 – 430	394	Possess beta-glucanase activity, but is unable to lyse viable cells
	Region	472 – 548	77	Essential for the lytic activity, but not for the beta-glucanase function

Sequences

	Sequence		Length	Mass (Da)
	P22222-1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 412B5A4AA24C048D	FASTA	548	58,089
	10 20 30 40 50 60 MPHDRKNSSR RAWAALCAAV LAVSGALVGV AAPASAVPAT IPLTITNDSG RGPIYLYVLG 70 80 90 100 110 120 ERDGVAGWAD AGGTFHPWPG GVGPVPVPAP DASIAGPGPG QSVTIRLPKL SGRVYYSYGQ 130 140 150 160 170 180 KMTFQIVLDG RLVQPAVQND SDPNRNILFN WTEYTLNDGG LWINSTQVDH WSAPYQVGVQ 190 200 210 220 230 240 RADGQVLSTG MLKPNGYEAF YTALEGAGWG GLVQRAPDGS RLRALNPSHG IDVGKISSAS 250 260 270 280 290 300 IDSYVTEVWN SYRTRDMVVT PFSHEPGTQF RGRVDGDWFR FRSGSGQEVA AFKKPDASSV 310 320 330 340 350 360 YGCHKDLQAP NDHVVGPIAR TLCAALVRTT ALTNPNQPDA NSAGFYQDAR TNVYAKLAHQ 370 380 390 400 410 420 QMANGKAYAF AFDDVGAHES LVHDGNPQAA YIKLDPFTGT ATPLGNGGST EQPGTPGGLP 430 440 450 460 470 480 AGTGALRIGS TLCLDVPWAD PTDTNQVQLA TCSGNAAQQW TRGTDGTVRA LGKCLDVARS 490 500 510 520 530 540 GTADGTAVWI YTCNGTGAQK WTYDSATKAL RNPQSGKCLD AQGGAPLRDG QKVQLWTCNQ TEAQRWTL

References

[1]

"Primary sequence of the glucanase gene from Oerskovia xanthineolytica. Expression and purification of the enzyme from Escherichia coli." Shen S.-H., Chretien P., Bastien L., Slilaty S.N. J. Biol. Chem. 266:1058-1063(1991) [PubMed: 1985933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 37-63, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M60826 Genomic DNA. Translation: AAA25520.1.
PIR	A39094.
3D structure databases
HSSP	HSSP built from PDB template 1KNM based on UniProtKB P26514.
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GH64. Glycoside Hydrolase Family 64.
Enzyme and pathway databases
BRENDA	3.2.1.39. 290399.
Family and domain databases
InterPro	IPR000772. Ricin_B_lectin. IPR017909. Twin_arg_translocation_Tat. [Graphical view]
Pfam	PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
SMART	SM00458. RICIN. 1 hit. [Graphical view]
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

E13B_CELCE

Accession

Primary (citable) accession number: P22222

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	June 16, 2009
This is version 61 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)