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P22222 (E13B_CELCE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismCellulosimicrobium cellulans (Arthrobacter luteus)
Taxonomic identifier1710 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaePromicromonosporaceaeCellulosimicrobium

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processCell wall biogenesis/degradation
   Cellular componentPeriplasm
   DomainSignal
   LigandLectin
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucan endo-1,3-beta-D-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636Tat-type signal Ref.1
Chain37 – 548512Glucan endo-1,3-beta-glucosidase
PRO_0000012235

Regions

Domain422 – 548127Ricin B-type lectin
Region37 – 430394Possess beta-glucanase activity, but is unable to lyse viable cells
Region472 – 54877Essential for the lytic activity, but not for the beta-glucanase function

Sequences

Sequence LengthMass (Da)Tools
P22222 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 412B5A4AA24C048D

FASTA54858,089
        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 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 37-63, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60826 Genomic DNA. Translation: AAA25520.1.
PIRA39094.

3D structure databases

ProteinModelPortalP22222.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GH64. Glycoside Hydrolase Family 64.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000772. Ricin_B_lectin.
IPR006311. TAT_signal.
[Graphical view]
PfamPF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE13B_CELCE
AccessionPrimary (citable) accession number: P22222
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 16, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries