ID   CLPB_RICCN              Reviewed;         857 AA.
AC   Q92JK8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=RC0059;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(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; AE006914; AAL02597.1; -; Genomic_DNA.
DR   PIR; C97707; C97707.
DR   RefSeq; WP_010976745.1; NC_003103.1.
DR   AlphaFoldDB; Q92JK8; -.
DR   SMR; Q92JK8; -.
DR   GeneID; 928600; -.
DR   KEGG; rco:RC0059; -.
DR   PATRIC; fig|272944.4.peg.70; -.
DR   HOGENOM; CLU_005070_4_0_5; -.
DR   Proteomes; UP000000816; 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   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
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; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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..857
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191169"
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..857
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   857 AA;  95972 MW;  2D34E3A0BCE47C8A CRC64;
     MNIDKFTAHA KSVIASSQLL AAKNDHQQIL PLHLLSSLLS EETGIIQTLI NNTGGNINLL
     KDQVQLELNK IPKVQVEGGG QVYSSAEALK VLEKASSIAK DNGDSFVTIE RIFEALTYDN
     TIAGKILTNN GINNKKIATA ILQFRKGKKA DTESAENSYD ALKKYGRDVT ELAESGKLDP
     IIGRDEEIRR TVQVLSRRMK NNPVLIGEPG VGKTAIIEGL AQRIFSKDVP ESLINCRIIE
     LDMGALIAGA KYRGEFEERL KAVLSEIKES SGEIILFIDE LHLLVGTGKT DGAMDASNLL
     KPMLARGELH CIGATTLDEY RKYIEKDAAL ARRFQPVYVS EPTVEDTISI LRGIKEKYEL
     HHAVRISDSA IVAAATLSNR YITDRYLPDK AIDLIDEACS RMKIELSSKP EELDELDRRI
     IQIKIELAAL KKENDEHSKK KIEHLTTALE KLESQSYDMG AKWQAEKSKL QQTQKLKEEL
     DRSRNELERA ERDANLAKAS ELKYGIIPEI MKKLQEAESM DNKGLLKEIV SESDIASIIS
     RITGIPIDTM LSSERERLLV MEQKLRESVI GQDKAIKGVS DAVRRSRAGI QDINRPLGSF
     LFLGPTGVGK TELTKALAGF LFDDRNAILR IDMSEYMEKH AISRLIGAPP GYIGYDQGGV
     LTEAVRRRPY QVILFDEVEK AHPDIFNIML QILDEGRLTD SQGITVDFKN TIIVLTSNLG
     AEILVNQKED EDTYKVKDEV MEYVKAVFKP EFLNRLDEII LFHRLNRNNI HDIVKIQLES
     LKKILLAQNI ILEFDESALN YLAEKGYDPS FGARPLKRLI QREIQNNLAK MILAGEISSG
     KTVKINSKDK ELKVTMS
//