P22222 (E13B_CELCE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 75.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 | |
| 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) | |
| 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 |
| 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
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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. |
| PIR | A39094. |
3D structure databases | |
| ProteinModelPortal | P22222. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | CBM13. Carbohydrate-Binding Module Family 13. GH64. Glycoside Hydrolase Family 64. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR000772. Ricin_B_lectin. IPR006311. TAT_signal. [Graphical view] |
| Pfam | PF00652. Ricin_B_lectin. 1 hit. [Graphical view] |
| SMART | SM00458. RICIN. 1 hit. [Graphical view] |
| SUPFAM | SSF50370. RicinB_like. 1 hit. |
| 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 |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
