ID   CLPB_BDEBA              Reviewed;         855 AA.
AC   Q6MIV0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=Bd3048;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
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; BX842654; CAE80813.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6MIV0; -.
DR   SMR; Q6MIV0; -.
DR   STRING; 264462.Bd3048; -.
DR   PRIDE; Q6MIV0; -.
DR   EnsemblBacteria; CAE80813; CAE80813; Bd3048.
DR   KEGG; bba:Bd3048; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_7; -.
DR   OMA; ERMKAVM; -.
DR   Proteomes; UP000008080; 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..855
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191093"
FT   DOMAIN          1..142
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          1..66
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..142
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          155..336
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          337..547
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          513..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..765
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          766..855
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          387..521
FT                   /evidence="ECO:0000250"
FT   BINDING         202..209
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   855 AA;  95239 MW;  7CA64902FEC94AF5 CRC64;
     MTRKSQEAMQ AAARLAERKS SPSVEPEHLL MELVQQTEGI VPRILDKLNV PQAQFLAELR
     TKIDKFPQVT GGGQKMFASP RLEKIFQAAE TEAQEWGDSY ISTEHFFMAM LKGGDSELNG
     LFKKNKVTAE AARTALTEIR GKQKVTDDDP ENKYEVLNKY ARDLTALAAE GKLDPVVGRD
     EEIRRVVQVL SRRTKNNPVL IGEPGVGKTA IAEGLALRII KQDVPDNLIG KKLMSLDMGA
     LIAGAKYRGE FEDRLKAVIK EVTSSDGQII LFIDELHTLV GAGKTEGAMD AGQLLKPALA
     RGELRCIGAT TLDEYRKYIE KDAALERRFQ TVMVEEPSVE DAITILRGLK EKYEVHHGIR
     ITDAALVSAV KLSHRYITNR FLPDKAIDLI DEAASKLGIE TRSVPEEVDK IERELMQLRI
     EKEALKKEKD ESARERLAVI DKEITELNAK NQLLREQWEF EKGGIEGIKK LKADIEDLKV
     AVAKAEREGD LGKAAELKYG KLPEAEKKLK ALEERSKEGA KSSSENRMLK EEVGPEDVAE
     VVAKWTGIPV SKMLESESQK LLHMEDSLKH RVVGQDHALT IVADAIRRAR AEISDPNRPI
     GTFMFLGPTG VGKTETVKAL AEFLFDDEQA VVRIDMSEYM EKHAVSRLIG APPGYVGYEE
     GGQLTESVRR RPYSVVLLDE VEKAHPDVFN ILLQVLDDGR LTDGQGRTVD FKNTVLIMTS
     NVGSQSILDP GMSENQKREA VNEALRERFR PEFLNRIDEI VMFKSLGEAQ ISGIVKVQLD
     LVAQRLRAKK IGIDFNQEAI DFLAKKGYDP IYGARPLKRV IQTELLNPLS KEIISGKVKA
     GDTIHVKANG STLTF