ID   CLPB_TROWT              Reviewed;         705 AA.
AC   Q83FI1;
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=TWT_746;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(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; AE014184; AAO44843.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q83FI1; -.
DR   SMR; Q83FI1; -.
DR   STRING; 203267.TWT_746; -.
DR   PRIDE; Q83FI1; -.
DR   EnsemblBacteria; AAO44843; AAO44843; TWT_746.
DR   KEGG; twh:TWT_746; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_11; -.
DR   OMA; SKMMQGE; -.
DR   Proteomes; UP000002200; 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; 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;
KW   Reference proteome; Repeat; Stress response.
FT   CHAIN           1..705
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191199"
FT   REGION          1
FT                   /note="N-terminal"
FT                   /evidence="ECO:0000250"
FT   REGION          14..191
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          192..395
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          405..611
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          612..705
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          242..373
FT                   /evidence="ECO:0000250"
FT   BINDING         59..66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         455..462
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   705 AA;  78364 MW;  BF41F52FB4E827D5 CRC64;
     MCGGSFMSES QSELDKYGTN LTKTAATNKL DPVIGRDAEI RRVCQILSRR TKNNPVLIGS
     AGVGKTAIVE GLAQRIVAGD VPESLRNKEI VSLDLSALLA GASYRGEFEK RVKNLLEEIQ
     KSKVIIFIDE VHTLMSAGAA EGAIAAGNML KPLLARGELR LIGATTLDEY REHLEKDPAL
     ERRFQQVFVG EPNLEDCIAI MRGLKERYEA HHKVSISDTA LVTAVELSSR YITGRQLPDK
     AIDLLDEAAS SLRMEIDSSP VELDQLRREV DRLRLEELAL KSENDPTSEQ RLRSITNQLS
     GKQEMLNTLQ ASWNSERARL NQIGALKEQI DIAKQSADIA QREGRLEDAS RLLYATIPQL
     QKNLAEKLEE QDSAPLVSDQ VMPEDIASVV EGWTGIPVKK LMQKDAKQLL HLEEDLSKSV
     IAQKVAIGVI ADAVRRSRAG LSDPNRPSGT FLFLGPTGVG KTQLVKALAS LLYDGEIVRI
     DMSEYSEKFS ISRLIGAPPG YIGHESAGQL TESVRRRPYS VVLFDEAEKA HPEVFDILLQ
     VLDEGRLTDS HGRTVDFRNT IIVLTSNIGS RYLSDISLEA TTAHEYVNDE VRRTFRPEFL
     NRLDEIVIFE PLSQSDICQI VDLNIESLNK RIKDRRIVVT VSEDLRRWLS KSGYDVIYGA
     RPLRRLIQRE IEDRLAKLII EGLIHDGQTA SFDLSGGAVN AQVCS