ID   CLPB_RHOPA              Reviewed;         879 AA.
AC   Q6N1H2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=RPA4433;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(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; BX572607; CAE29874.1; -; Genomic_DNA.
DR   RefSeq; WP_011159967.1; NC_005296.1.
DR   AlphaFoldDB; Q6N1H2; -.
DR   SMR; Q6N1H2; -.
DR   STRING; 258594.RPA4433; -.
DR   PRIDE; Q6N1H2; -.
DR   EnsemblBacteria; CAE29874; CAE29874; RPA4433.
DR   GeneID; 66895574; -.
DR   KEGG; rpa:RPA4433; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_5; -.
DR   OMA; GPEHILM; -.
DR   PhylomeDB; Q6N1H2; -.
DR   BioCyc; RPAL258594:TX73_RS22645-MON; -.
DR   Proteomes; UP000001426; 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..879
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191168"
FT   DOMAIN          3..148
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          84..148
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          161..342
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          343..546
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          556..766
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          767..879
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   REGION          858..879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          393..525
FT                   /evidence="ECO:0000250"
FT   BINDING         208..215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         606..613
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   879 AA;  96671 MW;  58298F774F08DCE2 CRC64;
     MNVEKYTERV RGFIQSAQSL AMREGHQQFS PLHILKVLLD DSEGLAGGLI DRAGGNSRAI
     LKATEEALGK MPKVSGSGAG QVYLAPATAR AFDAAEKAAE KAGDSFVTVE RLLLALSLDK
     DSEAGQLLTK GGVTPQNLNA AINALRKGRT ADSATAENAY DALKKYARDL TQAARDGKLD
     PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAIVEG LALRILNGDV PESLKDKKLL
     ALDMGALIAG AKYRGEFEER LKAVLNEVTA AEGGIILFID EMHTLVGAGK ADGAMDASNL
     LKPALARGEL HCIGATTLDE YRKHVEKDAA LARRFQPVFV SEPTVEDTVS ILRGLKDKYE
     QHHGVRIADS ALVAAVTLSN RYITDRFLPD KAIDLMDEAA ARLKMQVDSK PEELDSMDRE
     IVRLKIEQEA LKKETDPGSK ARLVTLEKEL ADLEEKSAAL TQRWSAEKNK LSDAQKLKSE
     LDALRIELAN AQRRGEYQRA GELAYGRIPE LEKKIAEIEA NENSGAMVEE AVTANHIAQV
     VSRWTGVPVD KMLEGEKEKL LRMEEQLGQR VVGQFEAVHA VSTAVRRARA GLQDPNRPMG
     SFMFLGPTGV GKTELTKALA EYLFDDETAM VRIDMSEFME KHSVARLIGA PPGYVGYDEG
     GVLTEAVRRR PYQVILFDEI EKAHPDVFNV LLQVLDDGRL TDGQGRTVDF RNTLIVMTSN
     LGSEYLVNQP EGEDTGAVRE QVMGMVRAHF RPEFLNRVDE IILFHRLQKS EMGRIVDIQF
     ARLTKLLEDR KIVLDLDAAA RDWLAEKGWD PAYGARPLKR VIQRSVQDPL AEMILEGSVK
     DGDHVAISAE GGVLTFNGKP PHTAEVEPFT GRPPKRMLN