Q8KG79 (CLPB1_CHLTE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 54.
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: Probable chaperone protein ClpB 1 | ||||
| Gene names |
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| Organism | Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 194439 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum › ![]() |
Protein attributes
| Sequence length | 438 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK By similarity. |
| Subunit structure | Homohexamer. The oligomerization is ATP-dependent By similarity. |
| Subcellular location | Cytoplasm Probable. |
| Domain | The N-terminal domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer By similarity. |
| Sequence similarities | Belongs to the clpA/clpB family. |
| Caution | This protein is much smaller than the orthologs present in other bacteria; the N-terminal and NBD1 domains are missing. However, there is a paralog in the genome (clpB2) that encodes a protein which contains only the N-terminal and NBD1 domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Stress response |
| Cellular component | Cytoplasm |
| Domain | Coiled coil |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Chaperone |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | response to stress Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 438 | 438 | Probable chaperone protein ClpB 1 | PRO_0000191107 | |||||
Regions | |||||||||
| Nucleotide binding | 178 – 185 | 8 | ATP Potential | ||||||
| Region | 1 – 118 | 118 | Linker By similarity | ||||||
| Region | 128 – 345 | 218 | NBD2 By similarity | ||||||
| Region | 346 – 438 | 93 | C-terminal By similarity | ||||||
| Coiled coil | 1 – 94 | 94 | By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE006470 Genomic DNA. Translation: AAM71337.1. |
| RefSeq | NP_660995.1. NC_002932.3. |
3D structure databases | |
| ProteinModelPortal | Q8KG79. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 194439.CT0089. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAM71337; AAM71337; CT0089. |
| GeneID | 1006510. |
| KEGG | cte:CT0089. |
| PATRIC | 21398281. VBIChlTep116050_0089. |
Phylogenomic databases | |
| eggNOG | COG0542. |
| HOGENOM | HOG000218211. |
| OMA | KRSRAGM. |
| ProtClustDB | CLSK637153. |
Enzyme and pathway databases | |
| BioCyc | CTEP194439:GHN0-90-MONOMER. |
Family and domain databases | |
| InterPro | IPR003593. AAA+_ATPase. IPR013093. ATPase_AAA-2. IPR001270. Chaprnin_ClpA/B. IPR019489. Clp_ATPase_C. [Graphical view] |
| Pfam | PF07724. AAA_2. 1 hit. PF10431. ClpB_D2-small. 1 hit. [Graphical view] |
| PRINTS | PR00300. CLPPROTEASEA. |
| SMART | SM00382. AAA. 1 hit. SM01086. ClpB_D2-small. 1 hit. [Graphical view] |
| PROSITE | PS00870. CLPAB_1. False negative. PS00871. CLPAB_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CLPB1_CHLTE | ||||||||
| Accession | Primary (citable) accession number: Q8KG79 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
