ID   CLPB_CHLTR              Reviewed;         867 AA.
AC   O84115;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=CT_113;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(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; AE001273; AAC67704.1; -; Genomic_DNA.
DR   PIR; D71555; D71555.
DR   RefSeq; NP_219616.1; NC_000117.1.
DR   RefSeq; WP_010725067.1; NC_000117.1.
DR   AlphaFoldDB; O84115; -.
DR   SMR; O84115; -.
DR   STRING; 813.O172_00615; -.
DR   EnsemblBacteria; AAC67704; AAC67704; CT_113.
DR   GeneID; 884031; -.
DR   KEGG; ctr:CT_113; -.
DR   PATRIC; fig|272561.5.peg.124; -.
DR   HOGENOM; CLU_005070_4_0_0; -.
DR   InParanoid; O84115; -.
DR   OMA; SKMMQGE; -.
DR   Proteomes; UP000000431; 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   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;
KW   Reference proteome; Repeat; Stress response.
FT   CHAIN           1..867
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191109"
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..867
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   867 AA;  96630 MW;  4B5A98F587BA7BAC CRC64;
     MEKFSDAVSE ALEKAFELAK NSKHSYVTEN HLLKSLLQNP GSLFCLVIKD VHGNLGLLTS
     AVDDALRREP TVVEGTAVAS PSPSLQQLLL NAHQEARSMG DEYLSGDHLL LAFWRSTKEP
     FASWRKTVKT TSEALKELIT KLRQGSRMDS PSAEENLKGL EKYCKNLTVL AREGKLDPVI
     GRDEEIRRTI QVLSRRTKNN PMLIGEPGVG KTAIAEGLAL RIVQGDVPES LKEKHLYVLD
     MGALIAGAKY RGEFEERLKS VLKGVEASEG ECILFIDEVH TLVGAGATDG AMDAANLLKP
     ALARGTLHCI GATTLNEYQK YIEKDAALER RFQPIFVTEP SLEDAVFILR GLREKYEIFH
     GVRITEGALN AAVVLSYRYI TDRFLPDKAI DLIDEAASLI RMQIGSLPLP IDEKERELSA
     LIVKQEAIKR EQAPAYQEEA EDMQKAIDRV KEELAALRLR WDEEKGLITG LKEKKNALEN
     LKFAEEEAER TADYNRVAEL RYSLIPSLEE EIHLAEEALN QRDGRLLQEE VDERLIAQVV
     ANWTGIPVQK MLEGESEKLL VLEESLEERV VGQPFAIAAV SDSIRAARVG LSDPQRPLGV
     FLFLGPTGVG KTELAKALAE LLFNKEEAMI RFDMTEYMEK HSVSKLIGSP PGYVGYEEGG
     SLSEALRRRP YSVVLFDEIE KADKEVFNIL LQIFDDGILT DSKKRKVNCK NALFIMTSNI
     GSQELADYCT KKGTIVDKEA VLSVVAPALK NYFSPEFINR IDDILPFVPL TTEDIVKIVG
     IQMNRVALRL LERKISLTWD DSLVLFLSEQ GYDSAFGARP LKRLIQQKVV TMLSKALLKG
     DIKPGMAVEL TMAKDVVVFK IKTNPAV