ID CLPB_BRADU Reviewed; 879 AA.
AC Q89UL2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=blr1404;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC46669.1; -; Genomic_DNA.
DR RefSeq; NP_768044.1; NC_004463.1.
DR RefSeq; WP_011084221.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89UL2; -.
DR SMR; Q89UL2; -.
DR STRING; 224911.AAV28_03935; -.
DR EnsemblBacteria; BAC46669; BAC46669; BAC46669.
DR GeneID; 64021274; -.
DR KEGG; bja:blr1404; -.
DR PATRIC; fig|224911.44.peg.828; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_5; -.
DR InParanoid; Q89UL2; -.
DR OrthoDB; 9803641at2; -.
DR PhylomeDB; Q89UL2; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..879
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191098"
FT DOMAIN 3..148
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 84..148
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 161..342
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 343..546
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 556..766
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 767..879
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 393..525
FT /evidence="ECO:0000250"
FT BINDING 208..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 606..613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 879 AA; 96622 MW; 0F935D239D7A3867 CRC64;
MNIEKYTERS RGFIQSAQSL AVREGHQQFS TLHVLKVLLD DNEGLAAGLI DRAGGNSRAI
LKATEDALNK VPKVSGGGAG QIYLAPELAR TFDAAEKAGE KAGDSFVTVE RLLLGLTLEK
TSEAGTILSK GGVTPQNLNA AIEALRKGRT ADSATAENAY DALKKYARDL TQAARDGKLD
PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAIAEG LALRIVNGDV PESLKDKKLL
SLDLGALIAG AKYRGEFEER LKAVLQEVTG SEGTFILFID EMHTLIGAGK GDGAMDASNL
LKPALARGEL HCIGATTLDE YQKHVEKDAA LARRFQPIFV SEPSVEDTIS ILRGLKDKYE
QHHGVRITDS ALVASATLSN RYITDRFLPD KAIDLMDEAA ARLKMQVDSK PEELDSMDRE
IIRLKIEQEA LKKESDAGSK SRLQTLEKEL VELEEKSASL TARWSAEKNK LSDAQKLKAE
LDGLRVELAN AQRRGEFQKA GELAYGRIPE LERQLADIEA KENSGEMMEE AVTANHIAQV
VSRWTGVPVD KMLEGEKDKL LKMEDSLGKR VVGQAEAVHA VATAVRRSRA GLQDPNRPMG
SFMFLGPTGV GKTELTKALA EYLFNDETAM VRLDMSEYME KHSVSRLIGA PPGYVGYDEG
GALTEAVRRR PYQVVLFDEI EKAHPDVFNV LLQVLDDGRL TDGQGRTVDF RNTLIIMTSN
LGSEFLVNQP EGEDTSAVRE QVMGMVRGHF RPEFLNRVDE IILFHRLQRS EMGRIVEIQF
ARLQKLLTDR KIVLTLDGAA RDWLAAKGWD PAYGARPLKR VIQRYLQDPL AEMILAGDVK
DGDNVAISSE GNVLTFNGKA PQTAEIAQFE APASKRKLN
//
