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Q9RA63 (CLPB_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chaperone protein ClpB
Gene names
Name:clpB
Ordered Locus Names:TTHA1487
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length854 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.1

Subunit structure

Homohexamer. The oligomerization is ATP-dependent. Ref.5 Ref.6

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.

Sequence similarities

Belongs to the ClpA/ClpB family.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-7698530,EBI-7698530
CSN3P026683EBI-7698530,EBI-7234047From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 854854Chaperone protein ClpB
PRO_0000191195

Regions

Nucleotide binding198 – 2058ATP 1
Nucleotide binding595 – 6028ATP 2
Region1 – 135135N-terminal
Region151 – 331181NBD1
Region332 – 535204Linker
Region545 – 756212NBD2
Region757 – 85498C-terminal
Coiled coil382 – 516135

Experimental info

Mutagenesis1671G → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-475. Ref.9
Mutagenesis204 – 2052KT → AA: Loss of ability to bind ATP. Residual ATPase activity.
Mutagenesis2701D → N: No effect on ability to bind ATP. Decrease in ATPase activity. Ref.6
Mutagenesis2711E → Q: No effect on ability to bind ATP. Increase in ATPase activity. Ref.6
Mutagenesis3501V → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-467. Ref.9
Mutagenesis3531G → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-464. Ref.9
Mutagenesis3551R → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-520. Ref.9
Mutagenesis3961L → A: Great decrease in chaperone activity. Retains ATPase activity and oligomerization. Ref.9
Mutagenesis4601L → A: Great decrease in chaperone activity. Retains ATPase activity and oligomerization. Ref.9
Mutagenesis4641R → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-353. Ref.9
Mutagenesis4671Q → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-350. Ref.9
Mutagenesis4751R → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-167. Ref.9
Mutagenesis5201E → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-355. Ref.9
Mutagenesis601 – 6022KT → AA: Loss of ability to bind ATP. Residual ATPase activity.
Mutagenesis6671D → N: Decrease in ATPase activity. Ref.6
Mutagenesis6681E → Q: Decrease in ATPase activity. Ref.6
Sequence conflict961A → G in BAA81745. Ref.1
Sequence conflict961A → G in BAA96085. Ref.1

Secondary structure

................................................................................................................................................. 854
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9RA63 [UniParc].

Last modified May 24, 2005. Version 2.
Checksum: FB9A39BB040363E0

FASTA85496,254
        10         20         30         40         50         60 
MNLERWTQAA REALAQAQVL AQRMKHQAID LPHLWAVLLK DERSLAWRLL EKAGADPKAL 

        70         80         90        100        110        120 
KELQERELAR LPKVEGAEVG QYLTSRLSGA LNRAEALMEE LKDRYVAVDT LVLALAEATP 

       130        140        150        160        170        180 
GLPGLEALKG ALKELRGGRT VQTEHAESTY NALEQYGIDL TRLAAEGKLD PVIGRDEEIR 

       190        200        210        220        230        240 
RVIQILLRRT KNNPVLIGEP GVGKTAIVEG LAQRIVKGDV PEGLKGKRIV SLQMGSLLAG 

       250        260        270        280        290        300 
AKYRGEFEER LKAVIQEVVQ SQGEVILFID ELHTVVGAGK AEGAVDAGNM LKPALARGEL 

       310        320        330        340        350        360 
RLIGATTLDE YREIEKDPAL ERRFQPVYVD EPTVEETISI LRGLKEKYEV HHGVRISDSA 

       370        380        390        400        410        420 
IIAAATLSHR YITERRLPDK AIDLIDEAAA RLRMALESAP EEIDALERKK LQLEIEREAL 

       430        440        450        460        470        480 
KKEKDPDSQE RLKAIEAEIA KLTEEIAKLR AEWEREREIL RKLREAQHRL DEVRREIELA 

       490        500        510        520        530        540 
ERQYDLNRAA ELRYGELPKL EAEVEALSEK LRGARFVRLE VTEEDIAEIV SRWTGIPVSK 

       550        560        570        580        590        600 
LLEGEREKLL RLEEELHKRV VGQDEAIRAV ADAIRRARAG LKDPNRPIGS FLFLGPTGVG 

       610        620        630        640        650        660 
KTELAKTLAA TLFDTEEAMI RIDMTEYMEK HAVSRLIGAP PGYVGYEEGG QLTEAVRRRP 

       670        680        690        700        710        720 
YSVILFDEIE KAHPDVFNIL LQILDDGRLT DSHGRTVDFR NTVIILTSNL GSPLILEGLQ 

       730        740        750        760        770        780 
KGWPYERIRD EVFKVLQQHF RPEFLNRLDE IVVFRPLTKE QIRQIVEIQL SYLRARLAEK 

       790        800        810        820        830        840 
RISLELTEAA KDFLAERGYD PVFGARPLRR VIQRELETPL AQKILAGEVK EGDRVQVDVG 

       850 
PAGLVFAVPA RVEA 

« Hide

References

« Hide 'large scale' references
[1]"Heat-inactivated proteins are rescued by the DnaK/J-GrpE set and ClpB chaperones."
Motohashi K., Watanabe Y.H., Yohda M., Yoshida M.
Proc. Natl. Acad. Sci. U.S.A. 96:7184-7189(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[3]"The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system."
Klostermeier D., Seidel R., Reinstein J.
J. Mol. Biol. 287:511-525(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-508.
[4]"Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form."
Watanabe Y.H., Motohashi K., Taguchi H., Yoshida M.
J. Biol. Chem. 275:12388-12392(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE DNAK-DNAJ-GRPE CHAPERONE SYSTEM.
[5]"The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites."
Schlee S., Groemping Y., Herde P., Seidel R., Reinstein J.
J. Mol. Biol. 306:889-899(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY CHARACTERIZATION OF SUBUNIT.
[6]"Roles of the two ATP binding sites of ClpB from Thermus thermophilus."
Watanabe Y.H., Motohashi K., Yoshida M.
J. Biol. Chem. 277:5804-5809(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF 204-LYS-THR-205; ASP-270; GLU-271; 601-LYS-THR-602; ASP-667 AND GLU-668.
[7]"A chaperone network for the resolubilization of protein aggregates: direct interaction of ClpB and DnaK."
Schlee S., Beinker P., Akhrymuk A., Reinstein J.
J. Mol. Biol. 336:275-285(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAK.
[8]"Crystallization and preliminary X-ray crystallographic analysis of the Hsp100 protein clpB from Thermus thermophilus."
Lee S., Hisayoshi M., Yoshida M., Tsai F.T.F.
Acta Crystallogr. D 59:2334-2336(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
[9]"The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state."
Lee S., Sowa M.E., Watanabe Y.H., Sigler P.B., Chiu W., Yoshida M., Tsai F.T.F.
Cell 115:229-240(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH AMPPNP, MUTAGENESIS OF GLY-167; VAL-350; GLY-353; ARG-355; LEU-396; LEU-460; ARG-464; GLN-467; ARG-475 AND GLU-520.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB012390 Genomic DNA. Translation: BAA81745.1.
AB032368 Genomic DNA. Translation: BAA96085.1.
AP008226 Genomic DNA. Translation: BAD71310.1.
Y07826 Genomic DNA. Translation: CAA69163.2.
RefSeqYP_144753.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QVRX-ray3.00A/B/C1-854[»]
4FCTX-ray4.00A545-852[»]
4FCVX-ray3.40A/B/C544-852[»]
4FCWX-ray2.35A/C/F544-852[»]
4FD2X-ray3.00A/B/D545-852[»]
4HSEX-ray2.20A142-534[»]
4LJ4X-ray2.80A520-854[»]
4LJ5X-ray2.40A520-854[»]
4LJ6X-ray1.90A520-854[»]
4LJ7X-ray2.80A/B/C520-854[»]
4LJ8X-ray2.10A520-854[»]
4LJ9X-ray1.70A520-854[»]
4LJAX-ray2.00A520-854[»]
ProteinModelPortalQ9RA63.
SMRQ9RA63. Positions 4-850.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-41758N.
IntActQ9RA63. 1 interaction.
MINTMINT-1131158.
STRING300852.TTHA1487.

PTM databases

PhosSiteP12101831.

Proteomic databases

PRIDEQ9RA63.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71310; BAD71310; BAD71310.
GeneID3167975.
KEGGttj:TTHA1487.
PATRIC23957935. VBITheThe93045_1462.

Phylogenomic databases

eggNOGCOG0542.
HOGENOMHOG000218211.
KOK03695.
OMAAKLSYQY.
OrthoDBEOG65F8SM.
ProtClustDBCLSK444852.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-1524-MONOMER.

Family and domain databases

Gene3D1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
IPR003959. ATPase_AAA_core.
IPR017730. Chaperonin_ClpB.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR001270. ClpA/B.
IPR018368. ClpA/B_CS1.
IPR028299. ClpA/B_CS2.
IPR023150. Dbl_Clp-N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSPR00300. CLPPROTEASEA.
SMARTSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
TIGRFAMsTIGR03346. chaperone_ClpB. 1 hit.
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9RA63.

Entry information

Entry nameCLPB_THET8
AccessionPrimary (citable) accession number: Q9RA63
Secondary accession number(s): P74942, Q5SI87
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 24, 2005
Last modified: April 16, 2014
This is version 98 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references