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Q9RA63

- CLPB_THET8

UniProt

Q9RA63 - CLPB_THET8

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
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (24 May 2005)
      Previous versions | rss
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    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
    3. nucleoside-triphosphatase activity Source: InterPro
    4. protein binding Source: IntAct

    GO - Biological processi

    1. protein processing Source: InterPro
    2. response to heat Source: InterPro

    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-SubCell

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

    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

    MNLERWTQAA REALAQAQVL AQRMKHQAID LPHLWAVLLK DERSLAWRLL    50
    EKAGADPKAL KELQERELAR LPKVEGAEVG QYLTSRLSGA LNRAEALMEE 100
    LKDRYVAVDT LVLALAEATP GLPGLEALKG ALKELRGGRT VQTEHAESTY 150
    NALEQYGIDL TRLAAEGKLD PVIGRDEEIR RVIQILLRRT KNNPVLIGEP 200
    GVGKTAIVEG LAQRIVKGDV PEGLKGKRIV SLQMGSLLAG AKYRGEFEER 250
    LKAVIQEVVQ SQGEVILFID ELHTVVGAGK AEGAVDAGNM LKPALARGEL 300
    RLIGATTLDE YREIEKDPAL ERRFQPVYVD EPTVEETISI LRGLKEKYEV 350
    HHGVRISDSA IIAAATLSHR YITERRLPDK AIDLIDEAAA RLRMALESAP 400
    EEIDALERKK LQLEIEREAL KKEKDPDSQE RLKAIEAEIA KLTEEIAKLR 450
    AEWEREREIL RKLREAQHRL DEVRREIELA ERQYDLNRAA ELRYGELPKL 500
    EAEVEALSEK LRGARFVRLE VTEEDIAEIV SRWTGIPVSK LLEGEREKLL 550
    RLEEELHKRV VGQDEAIRAV ADAIRRARAG LKDPNRPIGS FLFLGPTGVG 600
    KTELAKTLAA TLFDTEEAMI RIDMTEYMEK HAVSRLIGAP PGYVGYEEGG 650
    QLTEAVRRRP YSVILFDEIE KAHPDVFNIL LQILDDGRLT DSHGRTVDFR 700
    NTVIILTSNL GSPLILEGLQ KGWPYERIRD EVFKVLQQHF RPEFLNRLDE 750
    IVVFRPLTKE QIRQIVEIQL SYLRARLAEK RISLELTEAA KDFLAERGYD 800
    PVFGARPLRR VIQRELETPL AQKILAGEVK EGDRVQVDVG PAGLVFAVPA 850
    RVEA 854
    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

    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 1, 2014
    This is version 103 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