ID   CLPB_CLOAB              Reviewed;         865 AA.
AC   Q97KG0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=CA_C0959;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC       involved in the recovery of the cell from heat-induced damage, in
CC       cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The Clp repeat (R) domain probably functions as a substrate-
CC       discriminating domain, recruiting aggregated proteins to the ClpB
CC       hexamer and/or stabilizing bound proteins. The NBD2 domain is
CC       responsible for oligomerization, whereas the NBD1 domain stabilizes the
CC       hexamer probably in an ATP-dependent manner. The movement of the
CC       coiled-coil domain is essential for ClpB ability to rescue proteins
CC       from an aggregated state, probably by pulling apart large aggregated
CC       proteins, which are bound between the coiled-coils motifs of adjacent
CC       ClpB subunits in the functional hexamer (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR   EMBL; AE001437; AAK78935.1; -; Genomic_DNA.
DR   PIR; D97018; D97018.
DR   RefSeq; NP_347595.1; NC_003030.1.
DR   RefSeq; WP_010964277.1; NC_003030.1.
DR   AlphaFoldDB; Q97KG0; -.
DR   SMR; Q97KG0; -.
DR   STRING; 272562.CA_C0959; -.
DR   PRIDE; Q97KG0; -.
DR   EnsemblBacteria; AAK78935; AAK78935; CA_C0959.
DR   GeneID; 44997469; -.
DR   KEGG; cac:CA_C0959; -.
DR   PATRIC; fig|272562.8.peg.1168; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_9; -.
DR   OMA; GPEHILM; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017730; Chaperonin_ClpB.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81923; SSF81923; 1.
DR   TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; Repeat; Stress response.
FT   CHAIN           1..865
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191111"
FT   DOMAIN          3..150
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          6..71
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          86..150
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          163..344
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          345..551
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          561..772
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          773..865
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          395..529
FT                   /evidence="ECO:0000250"
FT   BINDING         210..217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         611..618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   865 AA;  97936 MW;  A00573DDE636118B CRC64;
     MDVDKLTLKV QQAINDCQTI AVRYNHQQID TIHLFMAIIS QEDGLIPNIL GKMGADVETV
     KRDTEAELDR MPKVLGEGAQ NASIYATRRF EEVFVRGEKI SRDFKDLYIS VEHVMLALMD
     IDSGAIKSIL DKNNISKKEF LKALREVRGN QRVDTSDPEG TYDALNKYGR DLVKDAKKHK
     LDPVIGRDEE IRRVIRILSR RTKNNPVLIG EPGVGKTAIV EGLAERIVRG DVPEGLKNKI
     IFSLDMGSLV AGAKYRGEFE ERLKAVLKEV ERSEGKIILF IDEIHTIVGA GKTEGAMDAG
     NIIKPMLARG ELHCIGATTF DEYRKYIEKD KALERRFQKV QIDEPTVDDA ISILRGLKER
     FEIHHGVRIH DNAIVAAAKL SDRYITGRFL PDKAIDLIDE AGAMVRMEID SMPTELDMLK
     RKIFQMEIEK EALSKESDKF SRERLESIQK ELSDLKDKDK AMTAKYDKEK AQIQGIKELK
     TKLDEIRGQI EKAEREYDLN KAAELKYGEV PKLEHEIEEK ENLIKQNGQN AMLKEEVTEE
     QVSNIVSKWT GIPVSKLVEG ERNKLMRLSD ELEKRVVGQT EAVKSVADAV IRARAGLKDM
     SKPIGSFIFL GPTGVGKTEL AKTLARVMFD SEDNIIRIDM SEYMEKYSVS RLIGSPPGYV
     GYEEGGQLTE AVRRKPYSVI LFDEIEKAHS DVFNIFLQIF DDGRLTDNKG NTIDFKNSII
     IMTSNIGSEH LLNNKGVSNV DEETKDKVMN ELKGRFKPEF LNRLDDIIMF KPLSINEIGK
     IIDIFLENIK SKLKEKNIKI DIAEEAKKII AEEGYDPVYG ARPLKRYIEN TIETHIAKMF
     ISGEISEGDI LKIEGSDSKL TIVKK