ID   CLPB_CHLMU              Reviewed;         867 AA.
AC   Q9PKS5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=TC_0389;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39246.1; -; Genomic_DNA.
DR   PIR; A81707; A81707.
DR   RefSeq; WP_010230340.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKS5; -.
DR   SMR; Q9PKS5; -.
DR   STRING; 243161.TC_0389; -.
DR   EnsemblBacteria; AAF39246; AAF39246; TC_0389.
DR   GeneID; 1245741; -.
DR   KEGG; cmu:TC_0389; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_0; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000000800; 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..867
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191105"
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;  96604 MW;  DAB4C579AAC79F57 CRC64;
     MEKFSDAVSE ALEKAFELAK DAKHSYVTEN HLLKSLLQNP GSLFCLVIKD VHGNLGLLTS
     AVDDALHREP TVVEGAAIPK PSPSLQQLLL NAQEEARSMG DEYLSGDHLL LAFWKTTKEP
     FASWRKTVKT SPEALKELII KLRQGSRMDS PSAEENLKGL EKYCKNLTIL AREGKLDPVI
     GRDEEIRRTI QVLSRRTKNN PMLIGEPGVG KTAIAEGLAL RIVQGDVPES LKDKHLYVLD
     MGALIAGAKY RGEFEERLKS VLKGVEASEG ACILFIDEVH TLVGAGATDG AMDAANLLKP
     ALARGTLHCI GATTLNEYQK YIEKDAALER RFQPIFVTEP SLEDAVFILR GLREKYEIFH
     GVRITEGALN AAVVLSYRYI TDRFLPDKAI DLIDEAASLI RMQIGSLPLP IDEKERELSA
     LIVKQEAIKR EQAPAYQEEA NEMQKAIDRV KEELAALRLR WDEEKGLIAG LKEKKNSLEN
     LKFAEEEAER TADYNRVAEL RYSLIPSLEK EIRLAEEALN QRDGRLLQEE VDERLIAQVV
     ANWTGIPVQK MLEGESEKLL VLEESLEERV VGQPFAITAV SDSIRSARVG LSDPQRPLGV
     FLFLGPTGVG KTELAKALAE LLFNKEEAMI RFDMTEYMEK HSVSKLIGSP PGYVGYEEGG
     SLSEALRRRP YSVVLFDEIE KADKEVFNIL LQIFDDGILT DSKKRKVNCK NALFIMTSNI
     GSQELADYCA KKGTIVDKEA VLSVVAPALK NYFSPEFINR IDEILPFVPL TTEDIVKIVG
     IQMNRVALRL LERRISLTWD DSVVLFLSEQ GYDGAFGARP LKRLIQQKVV TMLSKALLKG
     DIKSGMSVEL TMAKDVVVFK TKTNSVV