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Q9RA63

- CLPB_THET8

UniProt

Q9RA63 - CLPB_THET8

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Protein

Chaperone protein ClpB

Gene

clpB

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi198 – 2058ATP 1
Nucleotide bindingi595 – 6028ATP 2

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct

GO - Biological processi

  1. protein processing Source: InterPro
  2. response to heat Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1524-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein ClpB
Gene namesi
Name:clpB
Ordered Locus Names:TTHA1487
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi167 – 1671G → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-475. 1 Publication
Mutagenesisi204 – 2052KT → AA: Loss of ability to bind ATP. Residual ATPase activity. 1 Publication
Mutagenesisi270 – 2701D → N: No effect on ability to bind ATP. Decrease in ATPase activity. 1 Publication
Mutagenesisi271 – 2711E → Q: No effect on ability to bind ATP. Increase in ATPase activity. 1 Publication
Mutagenesisi350 – 3501V → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-467. 1 Publication
Mutagenesisi353 – 3531G → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-464. 1 Publication
Mutagenesisi355 – 3551R → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-520. 1 Publication
Mutagenesisi396 – 3961L → A: Great decrease in chaperone activity. Retains ATPase activity and oligomerization. 1 Publication
Mutagenesisi460 – 4601L → A: Great decrease in chaperone activity. Retains ATPase activity and oligomerization. 1 Publication
Mutagenesisi464 – 4641R → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-353. 1 Publication
Mutagenesisi467 – 4671Q → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-350. 1 Publication
Mutagenesisi475 – 4751R → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-167. 1 Publication
Mutagenesisi520 – 5201E → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-355. 1 Publication
Mutagenesisi601 – 6022KT → AA: Loss of ability to bind ATP. Residual ATPase activity. 1 Publication
Mutagenesisi667 – 6671D → N: Decrease in ATPase activity. 1 Publication
Mutagenesisi668 – 6681E → Q: Decrease in ATPase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 854854Chaperone protein ClpBPRO_0000191195Add
BLAST

Proteomic databases

PRIDEiQ9RA63.

PTM databases

PhosSiteiP12101831.

Interactioni

Subunit structurei

Homohexamer. The oligomerization is ATP-dependent.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-7698530,EBI-7698530
CSN3P026683EBI-7698530,EBI-7234047From a different organism.

Protein-protein interaction databases

DIPiDIP-41758N.
IntActiQ9RA63. 1 interaction.
MINTiMINT-1131158.
STRINGi300852.TTHA1487.

Structurei

Secondary structure

1
854
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2316Combined sources
Beta strandi27 – 293Combined sources
Helixi31 – 388Combined sources
Beta strandi41 – 444Combined sources
Helixi45 – 517Combined sources
Helixi57 – 6913Combined sources
Helixi76 – 783Combined sources
Helixi85 – 9915Combined sources
Turni100 – 1023Combined sources
Helixi108 – 11811Combined sources
Helixi125 – 1328Combined sources
Helixi152 – 1554Combined sources
Beta strandi156 – 1594Combined sources
Helixi160 – 1656Combined sources
Helixi176 – 18611Combined sources
Beta strandi188 – 1914Combined sources
Beta strandi193 – 1975Combined sources
Helixi204 – 21714Combined sources
Helixi222 – 2243Combined sources
Beta strandi228 – 2325Combined sources
Helixi234 – 2385Combined sources
Helixi246 – 26015Combined sources
Turni261 – 2633Combined sources
Beta strandi264 – 2718Combined sources
Helixi272 – 2743Combined sources
Helixi288 – 2969Combined sources
Beta strandi301 – 3066Combined sources
Helixi308 – 3158Combined sources
Helixi318 – 3214Combined sources
Beta strandi324 – 3285Combined sources
Helixi334 – 35219Combined sources
Helixi358 – 37114Combined sources
Helixi379 – 39719Combined sources
Helixi401 – 41919Combined sources
Helixi429 – 48355Combined sources
Helixi486 – 4938Combined sources
Helixi496 – 51217Combined sources
Beta strandi519 – 5213Combined sources
Helixi523 – 53412Combined sources
Helixi538 – 5414Combined sources
Helixi543 – 5497Combined sources
Helixi552 – 5576Combined sources
Helixi564 – 57815Combined sources
Beta strandi584 – 5863Combined sources
Beta strandi588 – 5958Combined sources
Beta strandi597 – 6004Combined sources
Helixi601 – 61313Combined sources
Helixi616 – 6183Combined sources
Beta strandi619 – 6235Combined sources
Helixi624 – 6263Combined sources
Helixi632 – 6376Combined sources
Beta strandi641 – 6433Combined sources
Turni644 – 6485Combined sources
Helixi651 – 6588Combined sources
Beta strandi663 – 6686Combined sources
Helixi669 – 6713Combined sources
Helixi674 – 68613Combined sources
Beta strandi687 – 6904Combined sources
Beta strandi692 – 6943Combined sources
Beta strandi696 – 6983Combined sources
Beta strandi703 – 7075Combined sources
Helixi712 – 72110Combined sources
Helixi725 – 73915Combined sources
Helixi742 – 7454Combined sources
Beta strandi748 – 7536Combined sources
Helixi759 – 76911Combined sources
Helixi771 – 7799Combined sources
Beta strandi783 – 7864Combined sources
Helixi788 – 79811Combined sources
Turni801 – 8033Combined sources
Turni805 – 8073Combined sources
Helixi808 – 8158Combined sources
Helixi817 – 8259Combined sources
Beta strandi827 – 8293Combined sources
Beta strandi834 – 8396Combined sources
Beta strandi841 – 8477Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9RA63.
SMRiQ9RA63. Positions 4-850.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RA63.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 135135N-terminalAdd
BLAST
Regioni151 – 331181NBD1Add
BLAST
Regioni332 – 535204LinkerAdd
BLAST
Regioni545 – 756212NBD2Add
BLAST
Regioni757 – 85498C-terminalAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili382 – 516135Add
BLAST

Domaini

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 similaritiesi

Belongs to the ClpA/ClpB family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG0542.
HOGENOMiHOG000218211.
KOiK03695.
OMAiEINHIVE.
OrthoDBiEOG65F8SM.
PhylomeDBiQ9RA63.

Family and domain databases

Gene3Di1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
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]
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSiPR00300. CLPPROTEASEA.
SMARTiSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR03346. chaperone_ClpB. 1 hit.
PROSITEiPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9RA63-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNLERWTQAA REALAQAQVL AQRMKHQAID LPHLWAVLLK DERSLAWRLL
60 70 80 90 100
EKAGADPKAL KELQERELAR LPKVEGAEVG QYLTSRLSGA LNRAEALMEE
110 120 130 140 150
LKDRYVAVDT LVLALAEATP GLPGLEALKG ALKELRGGRT VQTEHAESTY
160 170 180 190 200
NALEQYGIDL TRLAAEGKLD PVIGRDEEIR RVIQILLRRT KNNPVLIGEP
210 220 230 240 250
GVGKTAIVEG LAQRIVKGDV PEGLKGKRIV SLQMGSLLAG AKYRGEFEER
260 270 280 290 300
LKAVIQEVVQ SQGEVILFID ELHTVVGAGK AEGAVDAGNM LKPALARGEL
310 320 330 340 350
RLIGATTLDE YREIEKDPAL ERRFQPVYVD EPTVEETISI LRGLKEKYEV
360 370 380 390 400
HHGVRISDSA IIAAATLSHR YITERRLPDK AIDLIDEAAA RLRMALESAP
410 420 430 440 450
EEIDALERKK LQLEIEREAL KKEKDPDSQE RLKAIEAEIA KLTEEIAKLR
460 470 480 490 500
AEWEREREIL RKLREAQHRL DEVRREIELA ERQYDLNRAA ELRYGELPKL
510 520 530 540 550
EAEVEALSEK LRGARFVRLE VTEEDIAEIV SRWTGIPVSK LLEGEREKLL
560 570 580 590 600
RLEEELHKRV VGQDEAIRAV ADAIRRARAG LKDPNRPIGS FLFLGPTGVG
610 620 630 640 650
KTELAKTLAA TLFDTEEAMI RIDMTEYMEK HAVSRLIGAP PGYVGYEEGG
660 670 680 690 700
QLTEAVRRRP YSVILFDEIE KAHPDVFNIL LQILDDGRLT DSHGRTVDFR
710 720 730 740 750
NTVIILTSNL GSPLILEGLQ KGWPYERIRD EVFKVLQQHF RPEFLNRLDE
760 770 780 790 800
IVVFRPLTKE QIRQIVEIQL SYLRARLAEK RISLELTEAA KDFLAERGYD
810 820 830 840 850
PVFGARPLRR VIQRELETPL AQKILAGEVK EGDRVQVDVG PAGLVFAVPA

RVEA
Length:854
Mass (Da):96,254
Last modified:May 24, 2005 - v2
Checksum:iFB9A39BB040363E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961A → G in BAA81745. (PubMed:10377389)Curated
Sequence conflicti96 – 961A → G in BAA96085. (PubMed:10377389)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB012390 Genomic DNA. Translation: BAA81745.1.
AB032368 Genomic DNA. Translation: BAA96085.1.
AP008226 Genomic DNA. Translation: BAD71310.1.
Y07826 Genomic DNA. Translation: CAA69163.2.
RefSeqiWP_011228712.1. NC_006461.1.
YP_144753.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71310; BAD71310; BAD71310.
GeneIDi3167975.
KEGGittj:TTHA1487.
PATRICi23957935. VBITheThe93045_1462.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB012390 Genomic DNA. Translation: BAA81745.1 .
AB032368 Genomic DNA. Translation: BAA96085.1 .
AP008226 Genomic DNA. Translation: BAD71310.1 .
Y07826 Genomic DNA. Translation: CAA69163.2 .
RefSeqi WP_011228712.1. NC_006461.1.
YP_144753.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QVR X-ray 3.00 A/B/C 1-854 [» ]
4FCT X-ray 4.00 A 545-852 [» ]
4FCV X-ray 3.40 A/B/C 544-852 [» ]
4FCW X-ray 2.35 A/C/F 544-852 [» ]
4FD2 X-ray 3.00 A/B/D 545-852 [» ]
4HSE X-ray 2.20 A 142-534 [» ]
4LJ4 X-ray 2.80 A 520-854 [» ]
4LJ5 X-ray 2.40 A 520-854 [» ]
4LJ6 X-ray 1.90 A 520-854 [» ]
4LJ7 X-ray 2.80 A/B/C 520-854 [» ]
4LJ8 X-ray 2.10 A 520-854 [» ]
4LJ9 X-ray 1.70 A 520-854 [» ]
4LJA X-ray 2.00 A 520-854 [» ]
ProteinModelPortali Q9RA63.
SMRi Q9RA63. Positions 4-850.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-41758N.
IntActi Q9RA63. 1 interaction.
MINTi MINT-1131158.
STRINGi 300852.TTHA1487.

PTM databases

PhosSitei P12101831.

Proteomic databases

PRIDEi Q9RA63.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD71310 ; BAD71310 ; BAD71310 .
GeneIDi 3167975.
KEGGi ttj:TTHA1487.
PATRICi 23957935. VBITheThe93045_1462.

Phylogenomic databases

eggNOGi COG0542.
HOGENOMi HOG000218211.
KOi K03695.
OMAi EINHIVE.
OrthoDBi EOG65F8SM.
PhylomeDBi Q9RA63.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-1524-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9RA63.

Family and domain databases

Gene3Di 1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR003593. AAA+_ATPase.
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 ]
Pfami PF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view ]
PRINTSi PR00300. CLPPROTEASEA.
SMARTi SM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
TIGRFAMsi TIGR03346. chaperone_ClpB. 1 hit.
PROSITEi PS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiCLPB_THET8
AccessioniPrimary (citable) accession number: Q9RA63
Secondary accession number(s): P74942, Q5SI87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 24, 2005
Last modified: October 29, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3