ID   CLPB_CHLCV              Reviewed;         864 AA.
AC   Q822Q4;
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=CCA_00625;
OS   Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS   (Chlamydophila caviae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=227941;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX   PubMed=12682364; DOI=10.1093/nar/gkg321;
RA   Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA   Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA   Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA   Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA   Fraser C.M.;
RT   "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT   examining the role of niche-specific genes in the evolution of the
RT   Chlamydiaceae.";
RL   Nucleic Acids Res. 31:2134-2147(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; AE015925; AAP05367.1; -; Genomic_DNA.
DR   RefSeq; WP_011006582.1; NC_003361.3.
DR   AlphaFoldDB; Q822Q4; -.
DR   SMR; Q822Q4; -.
DR   STRING; 227941.CCA_00625; -.
DR   EnsemblBacteria; AAP05367; AAP05367; CCA_00625.
DR   KEGG; cca:CCA_00625; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_0; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000002193; 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   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; 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   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..864
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191104"
FT   DOMAIN          1..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          4..69
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          81..145
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          158..339
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          340..545
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          555..769
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          770..864
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          390..524
FT                   /evidence="ECO:0000250"
FT   BINDING         205..212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         605..612
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   864 AA;  96869 MW;  4DA3B0232FF2D98B CRC64;
     MDKISDAVSE ALEKAFELAQ SAKNPYVSEN HFLKCLLENT ESLFYLIIKD IHNNPKLLTS
     AVDEALSLEP SVIEGSAMPK PSPGLQSLLL DAKQEAKDLG DEYLSGDHVL LAFWKSNKEP
     FASWKKTVKI SLDDLKKLII NIRRGNRMDS PSAENNLRGL EKYCKNLTLL AKEGKLDPVI
     GRDEEIRRTV QVLSRRTKNN PMLIGEPGVG KTAIAEGLAL RIVQGDIPES LKGKQLYVLD
     MGALIAGAKY RGEFEERLKS VLKDVESVDG ESILFIDEVH TLVGAGATDG AMDAANLLKP
     ALARGTLHCI GATTLNEYQK YIEKDAALER RFQPIFVTEP SLEDAVFILR GLREKYEIFH
     GVRITEGALN AAVLLSYRYI PDRFLPDKAI DLIDEAASLI RMQIGSLPLP IDEKERELAA
     LIVKQEAIKR EKAPSYQEEA AAMQQSIEQL KEELAALRLR WDEEKKLITG LKEKKNSLEN
     MKFSEEEAER VADYNRVAEL RYSLIPALEE EIREDEEALN QRDNRLLQEE VDERLIAQVV
     ANWTGIPIQK MLEGEAEKLL VLEESLEERV VGQPFAISAV SDSIRAARVG LSDPQRPLGV
     FLFLGPTGVG KTELAKALAD LLFNKEEAMV RFDMTEYMEK HSVSKLIGSP PGYVGYEEGG
     SLSEALRRRP YSVVLFDEIE KADKEVFNIL LQIFDEGILT DSKKRKVNCK NALFIMTSNI
     GSQELADYCA KKGSRVSKET VLSVVAPTLK KYFSPEFINR IDDILPFVPL NTEDIVKIVG
     IQMRRVAQRL LERRVTLTWD DSVILYLSEQ GYDSSFGARP LKRLIQQKVV TLLSKALLKG
     DIKSDTSIEL TMSKDVLLFK KIEG