P0C2S1 (CELK_CLOTM) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 30.
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: Cellulose 1,4-beta-cellobiosidase EC=3.2.1.91 | ||
| Gene names |
| ||
| Organism | Clostridium thermocellum | ||
| Taxonomic identifier | 1515 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium![]() |
Protein attributes
| Sequence length | 895 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)
| Catalytic activity | Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains. Ref.1 |
| Enzyme regulation | Inhibited by cellobiose. Ref.1 |
| Subcellular location | |
| Sequence similarities | Belongs to the glycosyl hydrolase 9 (cellulase E) family. Contains 1 CBM-cenC (cenC-type cellulose-binding) domain. Contains 2 dockerin domains. |
| Biophysicochemical properties | Kinetic parameters: KM=1.67 µM for PNP-cellobioside Ref.1 Vmax=15.1 µmol/min/mg enzyme pH dependence: Optimum pH is 6.0. Temperature dependence: Retains 97% of original activity when incubated for 200 hours at 60 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Polysaccharide degradation |
| Cellular component | Secreted |
| Domain | Repeat Signal |
| Molecular function | Glycosidase Hydrolase |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | polysaccharide catabolic process Inferred from direct assay Ref.1. Source: UniProtKB |
| Cellular_component | extracellular space Inferred from direct assay Ref.2. Source: UniProtKB |
| Molecular_function | cellulase activity Inferred from electronic annotation. Source: InterPro cellulose 1,4-beta-cellobiosidase activityInferred from direct assay Ref.1. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 27 | 27 | Ref.2 | |||||||||||||||||||||||||||||||||||
| Chain | 28 – 895 | 868 | Cellulose 1,4-beta-cellobiosidase | PRO_0000045748 | ||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||
| Domain | 40 – 199 | 160 | CBM-cenC | |||||||||||||||||||||||||||||||||||
| Domain | 834 – 854 | 21 | Dockerin 1 | |||||||||||||||||||||||||||||||||||
| Domain | 866 – 886 | 21 | Dockerin 2 | |||||||||||||||||||||||||||||||||||
| Region | 199 – 240 | 42 | Linker | |||||||||||||||||||||||||||||||||||
| Region | 241 – 815 | 575 | Catalytic | |||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||
| Active site | 737 | 1 | By similarity | |||||||||||||||||||||||||||||||||||
| Active site | 786 | 1 | By similarity | |||||||||||||||||||||||||||||||||||
| Active site | 795 | 1 | By similarity | |||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 33 – 35 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 38 – 40 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 57 – 60 | 4 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 64 – 72 | 9 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 80 – 89 | 10 | ||||||||||||||||||||||||||||||||||||
| Helix | 93 – 95 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 96 – 105 | 10 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 110 – 121 | 12 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 123 – 133 | 11 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 138 – 142 | 5 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 147 – 150 | 4 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 153 – 162 | 10 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 168 – 176 | 9 | ||||||||||||||||||||||||||||||||||||
| Helix | 179 – 181 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 184 – 197 | 14 | ||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Cloning and sequence analysis of a new cellulase gene encoding CelK, a major cellulosome component of Clostridium thermocellum: evidence for gene duplication and recombination." Kataeva I., Li X.L., Chen H., Choi S.-K., Ljungdahl L.G. J. Bacteriol. 181:5288-5295(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 283-287 AND 326-337, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. Strain: JW20. |
| [2] | "Dissociation of the cellulosome of Clostridium thermocellum in the presence of ethylenediaminetetraacetic acid occurs with the formation of trucated polypeptides." Choi S.K., Ljungdahl L.G. Biochemistry 35:4897-4905(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-45, SUBCELLULAR LOCATION. Strain: JW20. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF039030 Genomic DNA. Translation: AAC06139.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P0C2S1. | ||||||||||||
| SMR | P0C2S1. Positions 208-813, 831-895. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| CAZy | CBM4. Carbohydrate-Binding Module Family 4. GH9. Glycoside Hydrolase Family 9. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 1.10.1330.10. 1 hit. 1.50.10.10. 1 hit. 2.60.40.10. 1 hit. | ||||||||||||
| InterPro | IPR008928. 6-hairpin_glycosidase-like. IPR012341. 6hp_glycosidase. IPR016134. Cellulos_enz_dockerin_1. IPR002105. Cellulos_enz_dockerin_1_Ca-bd. IPR003305. CenC_carb-bd. IPR018242. Dockerin_1. IPR008979. Galactose-bd-like. IPR001701. Glyco_hydro_9. IPR018221. Glyco_hydro_9_AS. IPR004197. Glyco_hydro_9_Ig-like. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. [Graphical view] | ||||||||||||
| Pfam | PF02018. CBM_4_9. 1 hit. PF02927. CelD_N. 1 hit. PF00404. Dockerin_1. 2 hits. PF00759. Glyco_hydro_9. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF63446. Cellulos_enz_dockerin_1. 1 hit. SSF49785. Gal_bind_like. 1 hit. SSF48208. Glyco_trans_6hp. 1 hit. SSF81296. Ig_E-set. 1 hit. | ||||||||||||
| PROSITE | PS00448. CLOS_CELLULOSOME_RPT. 1 hit. PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit. PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P0C2S1. | ||||||||||||
Entry information
| Entry name | CELK_CLOTM | ||||||||
| Accession | Primary (citable) accession number: P0C2S1 Secondary accession number(s): O68438, Q10748, Q4CGG7 | ||||||||
| 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
