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Q72IK9 (CLPB_THET2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chaperone protein ClpB
Gene names
Name:clpB
Ordered Locus Names:TT_C1123
OrganismThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]
Taxonomic identifier262724 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus ›

Protein attributes

Sequence length854 AA.
Sequence statusComplete.
Protein existenceInferred 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

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 By similarity.

Sequence similarities

Belongs to the clpA/clpB family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
   DomainCoiled coil
Repeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein processing

Inferred from electronic annotation. Source: InterPro

response to heat

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 854854Chaperone protein ClpB
PRO_0000191194

Regions

Nucleotide binding198 – 2058ATP 1 By similarity
Nucleotide binding595 – 6028ATP 2 By similarity
Region1 – 135135N-terminal By similarity
Region151 – 331181NBD1 By similarity
Region332 – 535204Linker By similarity
Region545 – 756212NBD2 By similarity
Region757 – 85498C-terminal By similarity
Coiled coil382 – 513132 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q72IK9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 49C33E7D7E86A3BE

FASTA85496,141
        10         20         30         40         50         60 
MNLERWTQAA REALAQAQVL AQRMKHQAID LPHLWAVLLK DEGGLAWRLL EKAGADPKAL 

        70         80         90        100        110        120 
KELQERELSR 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017221 Genomic DNA. Translation: AAS81465.1.
RefSeqYP_005092.1. NC_005835.1.

3D structure databases

ProteinModelPortalQ72IK9.
SMRQ72IK9. Positions 4-850.
ModBaseSearch...

Protein-protein interaction databases

STRING262724.TTC1123.

Proteomic databases

PRIDEQ72IK9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS81465; AAS81465; TT_C1123.
GeneID2775172.
KEGGtth:TTC1123.
PATRIC23952653. VBITheThe54392_1116.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0542.
KOK03695.
OMAHEATETW.
ProtClustDBCLSK444852.

Enzyme and pathway databases

BioCycTTHE262724:GCAT-1136-MONOMER.

Family and domain databases

Gene3D1.10.1780.10. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
IPR003959. ATPase_AAA_core.
IPR018368. Chaperonin_ClpA/B_CS.
IPR017730. Chaperonin_ClpB.
IPR001270. Chaprnin_ClpA/B.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
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...

Entry information

Entry nameCLPB_THET2
AccessionPrimary (citable) accession number: Q72IK9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 5, 2004
Last modified: May 29, 2013
This is version 60 of the entry and version 1 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

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