CLPB_THET2
ID CLPB_THET2 Reviewed; 854 AA.
AC Q72IK9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=TT_C1123;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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; AE017221; AAS81465.1; -; Genomic_DNA.
DR RefSeq; WP_011173537.1; NC_005835.1.
DR AlphaFoldDB; Q72IK9; -.
DR SMR; Q72IK9; -.
DR STRING; 262724.TT_C1123; -.
DR EnsemblBacteria; AAS81465; AAS81465; TT_C1123.
DR KEGG; tth:TT_C1123; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_0; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000000592; 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 GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; 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; IPR017730; Chaperonin_ClpB.
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 TIGRFAMs; TIGR03346; chaperone_ClpB; 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..854
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191194"
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..71
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 83..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 151..331
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 332..535
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 545..756
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 757..854
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 382..513
FT /evidence="ECO:0000250"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 595..602
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 854 AA; 96141 MW; 49C33E7D7E86A3BE CRC64;
MNLERWTQAA REALAQAQVL AQRMKHQAID LPHLWAVLLK DEGGLAWRLL EKAGADPKAL
KELQERELSR LPKVEGAEVG QYLTSRLSGA LNRAEALMEE LKDRYVAVDT LVLALAEATP
GLPGLEALKG ALKELRGGRT VQTEHAESTY NALEQYGIDL TRLAAEGKLD PVIGRDEEIR
RVIQILLRRT KNNPVLIGEP GVGKTAIVEG LAQRIVKGDV PEGLKGKRIV SLQMGSLLAG
AKYRGEFEER LKAVIQEVVQ SQGEVILFID ELHTVVGAGK AEGAVDAGNM LKPALARGEL
RLIGATTLDE YREIEKDPAL ERRFQPVYVD EPTVEETISI LRGLKEKYEV HHGVRISDSA
IIAAATLSHR YITERRLPDK AIDLIDEAAA RLRMALESAP EEIDALERKK LQLEIEREAL
KKEKDPDSQE RLKAIEAEIA KLTEEIAKLR AEWEREREIL RKLREAQHRL DEVRREIELA
ERQYDLNRAA ELRYGELPKL EAEVEALSEK LRGARFVRLE VTEEDIAEIV SRWTGIPVSK
LLEGEREKLL RLEEELHKRV VGQDEAIRAV ADAIRRARAG LKDPNRPIGS FLFLGPTGVG
KTELAKTLAA TLFDTEEAMI RIDMTEYMEK HAVSRLIGAP PGYVGYEEGG QLTEAVRRRP
YSVILFDEIE KAHPDVFNIL LQILDDGRLT DSHGRTVDFR NTVIILTSNL GSPLILEGLQ
KGWPYERIRD EVFKVLQQHF RPEFLNRLDE IVVFRPLTKE QIRQIVEIQL SYLRARLAEK
RISLELTEAA KDFLAERGYD PVFGARPLRR VIQRELETPL AQKILAGEVK EGDRVQVDVG
PAGLVFAVPA RVEA
