CLPB_MEIRU
ID CLPB_MEIRU Reviewed; 854 AA.
AC Q7X2S8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB;
OS Meiothermus ruber.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC Meiothermus.
OX NCBI_TaxID=277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12715159; DOI=10.1007/s00438-003-0818-2;
RA Pleckaityte M., Mistiniene E., Michailoviene V., Zvirblis G.;
RT "Identification and characterization of a Hsp70 (DnaK) chaperone system
RT from Meiothermus ruber.";
RL Mol. Genet. Genomics 269:109-115(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 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; AY303998; AAP59445.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7X2S8; -.
DR SMR; Q7X2S8; -.
DR PRIDE; Q7X2S8; -.
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_0000191138"
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; 94870 MW; 7315A53D2397A680 CRC64;
MNLERYTEQA RQAIAQSQVL ARESAHSKID LPHLAAVMLR DAAGLPAKIV QKAGQNPQNI
YQAAQSELGR LPKVSGTEGG QYLSSRLASA LGRAEKLADE LKDRFVALDT LLLALAETGY
GGLQASAVRQ ALQEIRGGRT VNSEHAEGTY NALEQYGLDL TRQAEEGKLD PVIGRDEEIR
RVIQILLRRT KNNPVLIGEP GVGKTAVVEG LAQRIVKGDV PEGLKGKRIV SLQMGSLLAG
AKYRGEFEER LKAVIQETVQ SAGQIILFID EIHTVVGAGK AEGAVDAGNM LKPALARGEL
HLIGATTLDE YREIEKDPAL ERRFQPVFVD EPSLEETVSI LRGIKEKYEV HHGVRISDPA
LIAAAQLSHR YIADRKLPDK AIDLVDEAAA RLRMALESSP ESIDALNRRK LQLEIEREAL
KKETDAESKF RLGELEKEIA DLEEEIRKQQ AEWEAEREIM QKLRAAQQRL DEVRTQIEQA
ERAYDLNKAA PLRYGELPKL EQEVNELADR MAGAQFVRPM VTEEDIAAIV SRWTGIPVAK
LMEGEREKLL RLEDELHKRV VGQDEAIVAV ADAIRRARAG LKDPNRPIGS FLFLGPTGVG
KTELAKTLAA SLFDTEENMV RIDMSEYQEK HTVARLIGAP PGYVGYEEGG QLTEAVRRRP
YSVILFDEIE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFR NTVIILTSNI GSPLIFEGIQ
SGQSYETIRE RVFGVLQQHF RPEFLNRLDE IVVFRPLARE QIAAIVQIQL EAVRKRLAER
RITLELSQEA LDFLAQRGYD PVFGARPLKR VIQRELETPL SRKILAGEVA DGAHLYVGSG
PLGLTFEARP TAVA
