ID   CLPB_TROW8              Reviewed;         699 AA.
AC   Q83N78;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=TW758;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(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 N-terminal 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; BX251412; CAD67417.1; -; Genomic_DNA.
DR   RefSeq; WP_011096695.1; NC_004551.1.
DR   AlphaFoldDB; Q83N78; -.
DR   SMR; Q83N78; -.
DR   PRIDE; Q83N78; -.
DR   GeneID; 67388539; -.
DR   KEGG; tws:TW758; -.
DR   HOGENOM; CLU_005070_4_0_11; -.
DR   OMA; SKMMQGE; -.
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; 3.40.50.300; -; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
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; 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   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..699
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191198"
FT   REGION          8..185
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          186..389
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          399..605
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          606..699
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          236..367
FT                   /evidence="ECO:0000250"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         449..456
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   699 AA;  77782 MW;  489FD8540EB647E7 CRC64;
     MSESQSELDK YGTNLTKTAA TNKLDPVIGR DAEIRRVCQI LSRRTKNNPV LIGSAGVGKT
     AIVEGLAQRI VAGDVPESLR NKEIVSLDLS ALLAGASYRG EFEKRVKNLL EEIQKSKVII
     FIDEVHTLMS AGAAEGAIAA GNMLKPLLAR GELRLIGATT LDEYREHLEK DPALERRFQQ
     VFVGEPNLED CIAIMRGLKE RYEAHHKVSI SDTALVTAVE LSSRYITGRQ LPDKAIDLLD
     EAASSLRMEI DSSPVELDQL RREVDRLRLE ELALKSENDP TSEQRLRSIT NQLSGKQEML
     NTLQASWNSE RARLNQIGAL KEQIDIAKQS ADIAQREGRL EDASRLLYAT IPQLQKNLAE
     KLEEQDSAPL VSDQVMPEDI ASVVEGWTGI PVKKLMQKDA KQLLHLEEDL SKSVIAQKVA
     IGVIADAVRR SRAGLSDPNR PSGTFLFLGP TGVGKTQLVK ALASLLYDGE IVRIDMSEYS
     EKFSISRLIG APPGYIGHES AGQLTESVRR RPYSVVLFDE AEKAHPEVFD ILLQVLDEGR
     LTDSHGRTVD FRNTIIVLTS NIGSRYLSDI SLEATTAHEY VNDEVRRTFR PEFLNRLDEI
     VIFEPLSQSD ICQIVDLNIE SLNKRIKDRR IVVTVSEDLR RWLSKSGYDV IYGARPLRRL
     IQREIEDRLA KLIIEGLIHD GQTASFDLSG GAVNAQVCS