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Protein

Chaperone protein ClpB

Gene

clpB

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Nucleotide bindingi198 – 205ATP 18
Nucleotide bindingi595 – 602ATP 28

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi167G → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-475. 1 Publication1
Mutagenesisi204 – 205KT → AA: Loss of ability to bind ATP. Residual ATPase activity. 1 Publication2
Mutagenesisi270D → N: No effect on ability to bind ATP. Decrease in ATPase activity. 1 Publication1
Mutagenesisi271E → Q: No effect on ability to bind ATP. Increase in ATPase activity. 1 Publication1
Mutagenesisi350V → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-467. 1 Publication1
Mutagenesisi353G → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-464. 1 Publication1
Mutagenesisi355R → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-520. 1 Publication1
Mutagenesisi396L → A: Great decrease in chaperone activity. Retains ATPase activity and oligomerization. 1 Publication1
Mutagenesisi460L → A: Great decrease in chaperone activity. Retains ATPase activity and oligomerization. 1 Publication1
Mutagenesisi464R → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-353. 1 Publication1
Mutagenesisi467Q → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-350. 1 Publication1
Mutagenesisi475R → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-167. 1 Publication1
Mutagenesisi520E → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-355. 1 Publication1
Mutagenesisi601 – 602KT → AA: Loss of ability to bind ATP. Residual ATPase activity. 1 Publication2
Mutagenesisi667D → N: Decrease in ATPase activity. 1 Publication1
Mutagenesisi668E → Q: Decrease in ATPase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001911951 – 854Chaperone protein ClpBAdd BLAST854

Proteomic databases

PRIDEiQ9RA63.

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.

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

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

Structurei

Secondary structure

1854
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 23Combined sources16
Beta strandi27 – 29Combined sources3
Helixi31 – 38Combined sources8
Beta strandi41 – 44Combined sources4
Helixi45 – 51Combined sources7
Helixi57 – 69Combined sources13
Helixi76 – 78Combined sources3
Helixi85 – 99Combined sources15
Turni100 – 102Combined sources3
Helixi108 – 118Combined sources11
Helixi125 – 132Combined sources8
Helixi152 – 155Combined sources4
Beta strandi156 – 159Combined sources4
Helixi160 – 165Combined sources6
Helixi176 – 186Combined sources11
Beta strandi188 – 191Combined sources4
Beta strandi193 – 197Combined sources5
Helixi204 – 217Combined sources14
Helixi222 – 224Combined sources3
Beta strandi228 – 232Combined sources5
Helixi234 – 238Combined sources5
Helixi246 – 260Combined sources15
Turni261 – 263Combined sources3
Beta strandi264 – 271Combined sources8
Helixi272 – 274Combined sources3
Helixi288 – 296Combined sources9
Beta strandi301 – 306Combined sources6
Helixi308 – 315Combined sources8
Helixi318 – 321Combined sources4
Beta strandi324 – 328Combined sources5
Helixi334 – 352Combined sources19
Helixi358 – 371Combined sources14
Helixi379 – 397Combined sources19
Helixi401 – 419Combined sources19
Helixi429 – 483Combined sources55
Helixi486 – 493Combined sources8
Helixi496 – 512Combined sources17
Beta strandi519 – 521Combined sources3
Helixi523 – 534Combined sources12
Helixi538 – 541Combined sources4
Helixi543 – 549Combined sources7
Helixi552 – 557Combined sources6
Helixi564 – 578Combined sources15
Beta strandi584 – 586Combined sources3
Beta strandi588 – 595Combined sources8
Beta strandi597 – 600Combined sources4
Helixi601 – 613Combined sources13
Helixi616 – 618Combined sources3
Beta strandi619 – 623Combined sources5
Helixi624 – 626Combined sources3
Helixi632 – 637Combined sources6
Beta strandi641 – 643Combined sources3
Turni644 – 648Combined sources5
Helixi651 – 658Combined sources8
Beta strandi663 – 668Combined sources6
Helixi669 – 671Combined sources3
Helixi674 – 686Combined sources13
Beta strandi687 – 690Combined sources4
Beta strandi692 – 694Combined sources3
Beta strandi696 – 698Combined sources3
Beta strandi703 – 707Combined sources5
Helixi712 – 721Combined sources10
Helixi725 – 739Combined sources15
Helixi742 – 745Combined sources4
Beta strandi748 – 753Combined sources6
Helixi759 – 769Combined sources11
Helixi771 – 779Combined sources9
Beta strandi783 – 786Combined sources4
Helixi788 – 798Combined sources11
Turni801 – 803Combined sources3
Turni805 – 807Combined sources3
Helixi808 – 815Combined sources8
Helixi817 – 825Combined sources9
Beta strandi827 – 829Combined sources3
Beta strandi834 – 839Combined sources6
Beta strandi841 – 847Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RA63.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 135N-terminalAdd BLAST135
Regioni151 – 331NBD1Add BLAST181
Regioni332 – 535LinkerAdd BLAST204
Regioni545 – 756NBD2Add BLAST212
Regioni757 – 854C-terminalAdd BLAST98

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili382 – 516Add BLAST135

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

eggNOGiENOG4105C2Z. Bacteria.
COG0542. LUCA.
HOGENOMiHOG000218211.
KOiK03695.
OMAiNIIRVDM.
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.
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.
SSF81923. SSF81923. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti96A → G in BAA81745 (PubMed:10377389).Curated1
Sequence conflicti96A → G in BAA96085 (PubMed:10377389).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PRIDEiQ9RA63.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105C2Z. Bacteria.
COG0542. LUCA.
HOGENOMiHOG000218211.
KOiK03695.
OMAiNIIRVDM.
PhylomeDBiQ9RA63.

Miscellaneous databases

EvolutionaryTraceiQ9RA63.

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.
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.
SSF81923. SSF81923. 1 hit.
TIGRFAMsiTIGR03346. chaperone_ClpB. 1 hit.
PROSITEiPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 116 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.