※ 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
 CA_C0959
Created Date
 3-June-2014
Organism
 Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
NCBI Taxa ID
 272562
Phosphorylation
Position
Peptide
Code
Type
References
643 IRIDMSEYMEKYSVS Y HTP [1]
641 NIIRIDMSEYMEKYS S HTP [1]
Reference
 [1]Phosphoproteomic investigation of a solvent producing bacterium Clostridium acetobutylicum.
 Bai X,Ji Z
 Appl. Microbiol. Biotechnol. 2012, Jul;95(1):201-11. [PMID:22627760]
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 (By similarity)
Sequence Annotation From UniProt
 COILED 395 529 By similarity
Key Word From UniProt
 ATP-binding; Chaperone; Coiledcoil; Completeproteome; Cytoplasm; Nucleotide-binding; Referenceproteome; Repeat; Stressresponse
Protein Sequence
 MDVDKLTLKV QQAINDCQTI AVRYNHQQID TIHLFMAIIS QEDGLIPNIL GKMGADVETV 60
 KRDTEAELDR MPKVLGEGAQ NASIYATRRF EEVFVRGEKI SRDFKDLYIS VEHVMLALMD 120
 IDSGAIKSIL DKNNISKKEF LKALREVRGN QRVDTSDPEG TYDALNKYGR DLVKDAKKHK 180
 LDPVIGRDEE IRRVIRILSR RTKNNPVLIG EPGVGKTAIV EGLAERIVRG DVPEGLKNKI 240
 IFSLDMGSLV AGAKYRGEFE ERLKAVLKEV ERSEGKIILF IDEIHTIVGA GKTEGAMDAG 300
 NIIKPMLARG ELHCIGATTF DEYRKYIEKD KALERRFQKV QIDEPTVDDA ISILRGLKER 360
 FEIHHGVRIH DNAIVAAAKL SDRYITGRFL PDKAIDLIDE AGAMVRMEID SMPTELDMLK 420
 RKIFQMEIEK EALSKESDKF SRERLESIQK ELSDLKDKDK AMTAKYDKEK AQIQGIKELK 480
 TKLDEIRGQI EKAEREYDLN KAAELKYGEV PKLEHEIEEK ENLIKQNGQN AMLKEEVTEE 540
 QVSNIVSKWT GIPVSKLVEG ERNKLMRLSD ELEKRVVGQT EAVKSVADAV IRARAGLKDM 600
 SKPIGSFIFL GPTGVGKTEL AKTLARVMFD SEDNIIRIDM SEYMEKYSVS RLIGSPPGYV 660
 GYEEGGQLTE AVRRKPYSVI LFDEIEKAHS DVFNIFLQIF DDGRLTDNKG NTIDFKNSII 720
 IMTSNIGSEH LLNNKGVSNV DEETKDKVMN ELKGRFKPEF LNRLDDIIMF KPLSINEIGK 780
 IIDIFLENIK SKLKEKNIKI DIAEEAKKII AEEGYDPVYG ARPLKRYIEN TIETHIAKMF 840
 ISGEISEGDI LKIEGSDSKL TIVKK 865
  GO:0005737   C:cytoplasm IEA:UniProtKB-SubCell
  GO:0005524   F:ATP binding IEA:UniProtKB-KW
  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.