ID   CLPB_COXBU              Reviewed;         859 AA.
AC   Q83F55;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=CBU_0094;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO89660.1; -; Genomic_DNA.
DR   RefSeq; NP_819146.1; NC_002971.3.
DR   RefSeq; WP_010957374.1; NZ_CCYB01000063.1.
DR   AlphaFoldDB; Q83F55; -.
DR   SMR; Q83F55; -.
DR   STRING; 227377.CBU_0094; -.
DR   EnsemblBacteria; AAO89660; AAO89660; CBU_0094.
DR   GeneID; 1207964; -.
DR   KEGG; cbu:CBU_0094; -.
DR   PATRIC; fig|227377.7.peg.95; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_6; -.
DR   OMA; SKMMQGE; -.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; 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..859
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191117"
FT   DOMAIN          3..146
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          83..146
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          159..340
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          341..547
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          557..766
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          767..859
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          391..525
FT                   /evidence="ECO:0000250"
FT   BINDING         206..213
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   859 AA;  96769 MW;  D0D834A1F973197D CRC64;
     MRIDKFTTAF QTALADAQSL AVGRDHQFIE PAHVMKVLLE QTQGTVAPLL EQSKVNLSRL
     IDGVNKAIDS YPQVEGTGGE VHVSRELSKI LTLMDKFAQQ NKDQYISSEW FIPAALEAKG
     QLRDVLIEAG ADKKAIEKNI MNLRKGERVT EQSAEDQRQA LAKYTIDLTE KAETGKLDPV
     IGRDEEIRRT VQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKQKRLLAL
     DMGALIAGAK FRGEFEERLK AVLKDIAKEE GRVILFIDEL HTMVGAGKAE GAMDAGNMLK
     PALARGELHC VGATTLDEYR KYIEKDAALE RRFQKVLVEE PSTEDAIAIL RGLKERYEVH
     HGVEITDPAI IAAATLSQRY ITDRNLPDKA IDLIDEAASQ IRMEMDSKPV ELDRLERRLI
     QLKIEREALK KETDEASKKR LSDLETEIKN VEKEYSDLEE VWKSEKASLH GTQQIKEELE
     QARIELEAAG RAGDLARMSE LQYGIIPELD KKLKAASQKE EQFHDHKLLR SRVTEEEVAE
     VVSKWTHIPV SKMLEGEREK LLHMETELHK RVIGQDEAVN AVANAIRRSR AGLSDPNRPV
     GSFLFLGPTG VGKTELCKAL AVFLFDTEDA MVRIDMSEFM EKHSVARLIG APPGYVGYEE
     GGYLTEAIRR RPYSVILLDE IEKAHNDVFN VLLQVLDDGR LTDGQGRTVD FRNTVIVMTS
     NLGSDLIREF SGENYDKMKD AVMEVVAQHF RPEFINRIDE AVVFHSLKKE QIRNIAIIQI
     DRIKKRLKEK DYQLTISDDA LDYLSELGYD PVYGARPLKR VLQQQLENPL SQKILEGKFV
     PGSLINIEKK GEQLEFKEA