Reviewed,
UniProtKB/Swiss-Prot Q83F55 (CLPB_COXBU)
Last modified
July 22, 2008.
Version 28.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Chaperone protein clpB | ||||
| Gene names |
| ||||
| Organism | Coxiella burnetii [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 777 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella |
Protein attributes
| Sequence length | 859 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 | CytoplasmProbable. |
| 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. |
Ontologies
Keywords | |
|---|---|
| Biological process | Stress response |
| Cellular component | Cytoplasm |
| Domain | Coiled coil Repeat |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Chaperone |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| None. [Check GOA] | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | ||||
Molecule processing | ||||||||
|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 859 | 859 | Chaperone protein clpB | |||||
Regions | ||||||||
| Nucleotide binding | 206 – 213 | 8 | ATP 1 By similarity | |||||
| Nucleotide binding | 607 – 614 | 8 | ATP 2 By similarity | |||||
| Region | 1 – 143 | 143 | N-terminal By similarity | |||||
| Region | 159 – 340 | 182 | NBD1 By similarity | |||||
| Region | 341 – 547 | 207 | Linker By similarity | |||||
| Region | 557 – 766 | 210 | NBD2 By similarity | |||||
| Region | 767 – 859 | 93 | C-terminal By similarity | |||||
| Coiled coil | 391 – 525 | 135 | By similarity | |||||
Sequences
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References
| [1] | "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. Heidelberg J.F.Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nine Mile phase I / RSA 493. |
Cross-references
Sequence databases | |
|---|---|
| AE016828 Genomic DNA. Translation: AAO89660.1. | |
| RefSeq | NP_819146.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JBK based on UniProtKB P03815. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1207964. |
| GenomeReviews | Gene locus CBU_0094 in contig AE016828_GR. |
| KEGG | cbu:CBU_0094. |
| NMPDR | fig|227377.1.peg.90. |
| TIGR | CBU_0094. |
Phylogenomic databases | |
| HOGENOM | Q83F55. |
Enzyme and pathway databases | |
| BioCyc | CBUR227377:CBU_0094-MON. |
Family and domain databases | |
| InterPro | IPR003593. AAA+_ATPase_core. IPR003959. AAA_ATPase_core. IPR013093. ATPase_AAA-2. IPR017730. Chaperonin_ClpB. IPR001270. Chaprnin_clpA/B. IPR004176. Clp_N. [Graphical view] |
| Pfam | PF00004. AAA. 1 hit. PF07724. AAA_2. 1 hit. PF02861. Clp_N. 2 hits. [Graphical view] |
| PRINTS | PR00300. CLPPROTEASEA. |
| SMART | SM00382. AAA. 2 hits. [Graphical view] |
| PROSITE | PS00870. CLPAB_1. 1 hit. PS00871. CLPAB_2. 1 hit. [Graphical view] |
| ProDom | Q83F55. [Graphical view] [Entries sharing at least one domain] |
| BLOCKS | Search... |
Other Resources | |
| ProtoNet | Search... |
Entry information
| Entry name | CLPB_COXBU | ||||||||
| Accession | Primary (citable) accession number: Q83F55 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Coxiella burnetii Coxiella burnetii (strain RSA 493): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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