ID   CLPB_RICPR              Reviewed;         858 AA.
AC   Q9ZEA9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=RP036;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235270; CAA14507.1; -; Genomic_DNA.
DR   PIR; D71711; D71711.
DR   RefSeq; NP_220430.1; NC_000963.1.
DR   RefSeq; WP_004596648.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZEA9; -.
DR   SMR; Q9ZEA9; -.
DR   STRING; 272947.RP036; -.
DR   PRIDE; Q9ZEA9; -.
DR   EnsemblBacteria; CAA14507; CAA14507; CAA14507.
DR   GeneID; 57569164; -.
DR   KEGG; rpr:RP036; -.
DR   PATRIC; fig|272947.5.peg.37; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_5; -.
DR   OMA; ERMKAVM; -.
DR   Proteomes; UP000002480; 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..858
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191170"
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;  96291 MW;  A18F52B6CD5805AE CRC64;
     MNIDKFTAHA KSVIANHQSL AIKNDHQQIL PLHLLSSLLS EETGIIQALI NNIGGNINLL
     KDQVQLELNK IPKIQVDGGG QIYYSAEDLK VLEKSSSIAK DSGDSFVTIE RIFEALTYDN
     TIAGKILTNN GINSKKLATA ILHLRKGKKA DTESAENNYD ALKRYGRDVT ELAENGKLDP
     IIGRDEEIRR AVQVLSRRMK NNPVLIGAPG VGKTAIIEGL AQRIFSKDVP ETLINCRIIE
     LDIGALIAGA QYRGEFEKRL KAVLSEIKES SGEIILFIDE LHLLVGTGKV DGAMDASNLL
     KPMLARGELH CIGATTLDEY RKYIEKDAAL ARRFQPVYVG EPSVEDTISI LRGIKEKYEL
     HHAVRISDSA IVAAATLSNR YITDRYLPDK AIDLIDEACS RMKIELSSKP EELDELDRRI
     IQIKIELAAL KKENDEHSKK KITSLTEELK KLESKSYDMN TKWQAEKSKL QQAQKLKEEL
     EQARIDLERA ERDANLAKAS ELKYGIIPEI MNKLQEAENM DNKGLLKEIV SESDIASIIS
     RITGIPIDTM LSSERERLLV IEQKLCESVI GQDEAIKGVS DAVRRSRSGI QDINRPLGSF
     LFLGPTGVGK TELTKALAGF LFDDRNALLR IDMSEYMEKH SISRLIGAPP GYIGYDQGGV
     LTESVRRRPY QVILFDEVEK AHLDIFNIML QILDEGRLTD SQGITVDFKN TIIVLTSNLG
     AEILVNQKEG EDTYKVRDEV MQYVRAVFKP EFLNRLDEII LFHRLNRNNI HDIVKIQLGS
     LKKILLQQNI ILEFDESALN YLAEKGYDPS FGARPLKRLI QREIQNNLAK MILAGEISSG
     NTVKIRREKE ELSINIID