ID   CLPB_RICBR              Reviewed;         858 AA.
AC   Q1RGR1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=RBE_1372;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05453.1; -; Genomic_DNA.
DR   RefSeq; WP_011478022.1; NC_007940.1.
DR   AlphaFoldDB; Q1RGR1; -.
DR   SMR; Q1RGR1; -.
DR   STRING; 336407.RBE_1372; -.
DR   EnsemblBacteria; ABE05453; ABE05453; RBE_1372.
DR   KEGG; rbe:RBE_1372; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_5; -.
DR   OMA; ERMKAVM; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000001951; 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; Repeat;
KW   Stress response.
FT   CHAIN           1..858
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000281060"
FT   DOMAIN          3..147
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..147
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          160..341
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          342..544
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          554..764
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          765..858
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          392..523
FT                   /evidence="ECO:0000250"
FT   BINDING         207..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         604..611
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   858 AA;  95940 MW;  C2B56A515C88CCDC CRC64;
     MNIDKFTAHA KSAITNCQHI AAKNDHQQIL PLHLLASLFN EDTGIIRTLI NNSGGNLNIL
     ADQVQVELNK IPKVQVDGGG TIYSSAELLK VLQRADDLAK NNGDSFVTIE RILEALSFDN
     TIAGKILTNN GISSKKLAAS ILQLRKGKKA DTESAENSYD ALKKYGRDVT ELAESGKLDP
     IIGRDEEIRR TVQVLSRRMK NNPVLIGEPG VGKTAIIEGL AQRIFSKDVP ETLINCRIIE
     LDMGALIAGA KYRGEFEERL KAVLGEIKES SGEIILFIDE LHLLVGTGKT DGAMDASNLL
     KPMLARGELH CIGATTLDEY RKYIEKDAAF ARRFQPVYVS EPTVEDTISI LRGIKEKYEL
     HHAVRISDSA IVAAATLSNR YITDRFLPDK AIDLIDEACS RMKIELSSKP EELDELDRRI
     IQIKIELAAL KKESDEHSKK KIEHLTAELE KLESNSYDMS SKWQAEKSKI QGQQKLKEEL
     DRARIDLERA ERDANLAKAS ELKYGIIPEI MKKIQETENA DSKGLLKEIV SESDIASIIS
     RITGIPIDTM LSSERERLLV MEQKLRESVI GQDEAIKSVS DAVRRSRAGI QDINRPLGSF
     LFLGPTGVGK TELTKALAGF LFDDRNAILR IDMSEYMEKH AISRLIGAPP GYVGYDQGGV
     LTEAVRRRPY QVILFDEVEK AHPDIFNIML QILDEGRLTD SQGITVDFKN TIIVLTSNLG
     AEILVNQKEG EDTYKVKDQV MEYVKMVFKP EFLNRLDEII LFHRLNQSNI HDIVKIQLEG
     LKKILSAQNI ILEFDEPALN YLAEKGYDPS FGARPLKRLI QREIQNNLAK MILAGEVSSG
     KIVKITAKKE ELKIQIID