ID   CLPB_BLOFL              Reviewed;         872 AA.
AC   Q7VQF3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=Bfl182;
OS   Blochmannia floridanus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=203907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis of
RT   reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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; BX248583; CAD83701.1; -; Genomic_DNA.
DR   RefSeq; WP_011126468.1; NC_005061.1.
DR   AlphaFoldDB; Q7VQF3; -.
DR   SMR; Q7VQF3; -.
DR   STRING; 203907.Bfl182; -.
DR   PRIDE; Q7VQF3; -.
DR   EnsemblBacteria; CAD83701; CAD83701; Bfl182.
DR   KEGG; bfl:Bfl182; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_6; -.
DR   OMA; ERMKAVM; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000002192; 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; 1.
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..872
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191102"
FT   DOMAIN          3..149
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          6..72
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          86..149
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          162..342
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          343..547
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          557..767
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          768..872
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          393..525
FT                   /evidence="ECO:0000250"
FT   BINDING         209..216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         607..614
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   872 AA;  99659 MW;  AD0F256AEC99B847 CRC64;
     MRLDRFDRSF QLALSDAQSI AIGKDNQFIE PVHVMYTFLK EKKYKSIRNL LIHAGSNVDQ
     LYKSVEQVCN DLPRVESVDG DREVQCSHAL VKILNLCDKL AQKYHSNIIF SEVFIIAALQ
     SQDVLSILLK KSGIVKELLE KLVQYEQSNY SIHDDSFKNR TQILEQFTVD ITSLAEQNNL
     DPVIGRDEEI RRTIQVLQRR TKNNPVLIGN PGVGKTAIVE GLAQRIINKE VPEGLKNSRI
     LSLDIAALLA GTKYRGEFEE RFKKVLYAVS KDNNTILFID ELHVMVGAGK TDGSMDASNM
     IKPKLARGEL HCVGATTLDE YSRYIEKDAA LERRFQKIFI IEPNIENTIA ILRGLKERYE
     LHHNVHITDP AIVAAATLSN RYISDRQLPD KAIDLIDEAA SSIRIQIDSK PEDLDRLDRR
     IIQLKLECQA LKKESDELSK KRLEILSMEL SQKEQEYSVL ESEWKRERSS LFDIQNIKSD
     LEKAKTILDQ SRRIGDLAQM SELQYGRIPE LEKKLFNAIQ SSNKKMRLLR NYVSEVEIAE
     VLSKWTGIPI SRILANEKNK LLNMETILHQ LVIGQDEAVR VISNAIRRSR SGLSDPKRPI
     GSFMFLGPTG VGKTELCKAL SQFLFDTDNA MVRIDMSEFM EKHSVSKLLG APPGYIGYES
     GAYLTESIRR RPYSIVLLDE IEKAHLDVFN ILLQVLDDGR LTDNQGRMVD FNNTVIIMTS
     NLGSDLIQKK FDISDYDTMK KTVLNVVNQY FRPEFINRID EIVVFHPLSI KHLIDIANIQ
     LKYLYSRLEE RGYPRTGITN KALLFLSKIG FDPIYGARPL KRIIQQYIEN PLSQKILSDD
     LLPGRSITID VQNDNIVFIQ NDVIDDKDIY IN