※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chaperone protein ClpB
Protein Synonyms/Alias
 
Gene Name
 clpB
Gene Synonyms/Alias
 TTHA1487
Created Date
 3-June-2014
Organism
 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
NCBI Taxa ID
 300852
Phosphorylation
Position
Peptide
Code
Type
References
85 EVGQYLTSRLSGALN S HTP [1]
Reference
 [1]Close proximity of phosphorylation sites to ligand in the phosphoproteome of the extreme thermophile Thermus thermophilus HB8.
 Takahata Y,Inoue M,Kim K,Iio Y,Miyamoto M,Masui R,Ishihama Y,Kuramitsu S
 Proteomics 2012, May;12(9):1414-30. [PMID:22589190]
Functional Description From UniProt
 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
Sequence Annotation From UniProt
 COILED 382 516
Key Word From UniProt
 3D-structure; ATP-binding; Chaperone; Coiledcoil; Completeproteome; Cytoplasm; Nucleotide-binding; Referenceproteome; Repeat; Stressresponse
Protein Sequence
 MNLERWTQAA REALAQAQVL AQRMKHQAID LPHLWAVLLK DERSLAWRLL EKAGADPKAL 60
 KELQERELAR LPKVEGAEVG QYLTSRLSGA LNRAEALMEE LKDRYVAVDT LVLALAEATP 120
 GLPGLEALKG ALKELRGGRT VQTEHAESTY NALEQYGIDL TRLAAEGKLD PVIGRDEEIR 180
 RVIQILLRRT KNNPVLIGEP GVGKTAIVEG LAQRIVKGDV PEGLKGKRIV SLQMGSLLAG 240
 AKYRGEFEER LKAVIQEVVQ SQGEVILFID ELHTVVGAGK AEGAVDAGNM LKPALARGEL 300
 RLIGATTLDE YREIEKDPAL ERRFQPVYVD EPTVEETISI LRGLKEKYEV HHGVRISDSA 360
 IIAAATLSHR YITERRLPDK AIDLIDEAAA RLRMALESAP EEIDALERKK LQLEIEREAL 420
 KKEKDPDSQE RLKAIEAEIA KLTEEIAKLR AEWEREREIL RKLREAQHRL DEVRREIELA 480
 ERQYDLNRAA ELRYGELPKL EAEVEALSEK LRGARFVRLE VTEEDIAEIV SRWTGIPVSK 540
 LLEGEREKLL RLEEELHKRV VGQDEAIRAV ADAIRRARAG LKDPNRPIGS FLFLGPTGVG 600
 KTELAKTLAA TLFDTEEAMI RIDMTEYMEK HAVSRLIGAP PGYVGYEEGG QLTEAVRRRP 660
 YSVILFDEIE KAHPDVFNIL LQILDDGRLT DSHGRTVDFR NTVIILTSNL GSPLILEGLQ 720
 KGWPYERIRD EVFKVLQQHF RPEFLNRLDE IVVFRPLTKE QIRQIVEIQL SYLRARLAEK 780
 RISLELTEAA KDFLAERGYD PVFGARPLRR VIQRELETPL AQKILAGEVK EGDRVQVDVG 840
 PAGLVFAVPA RVEA 854
  GO:0005737   C:cytoplasm IEA:UniProtKB-SubCell
  GO:0005524   F:ATP binding IEA:UniProtKB-KW
  GO:0042802   F:identical protein binding IPI:IntAct
  GO:0017111   F:nucleoside-triphosphatase activity IEA:InterPro
  GO:0016485   P:protein processing IEA:InterPro
  GO:0009408   P:response to heat IEA:InterPro
  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.
  PF00004   AAA.
  PF07724   AAA_2.
  PF02861   Clp_N.
  PF10431   ClpB_D2-small.
  SM00382   AAA.
  SM01086   ClpB_D2-small.
  PS00870   CLPAB_1.
  PS00871   CLPAB_2.
  PR00300   CLPPROTEASEA.