ID A0A4Q8QRJ9_9BRAD Unreviewed; 879 AA.
AC A0A4Q8QRJ9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TAI62471.1};
GN ORFNames=CWO89_29545 {ECO:0000313|EMBL:TAI62471.1};
OS Bradyrhizobium sp. Leo170.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1571199 {ECO:0000313|EMBL:TAI62471.1, ECO:0000313|Proteomes:UP000292824};
RN [1] {ECO:0000313|EMBL:TAI62471.1, ECO:0000313|Proteomes:UP000292824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leo170 {ECO:0000313|EMBL:TAI62471.1,
RC ECO:0000313|Proteomes:UP000292824};
RA Avontuur J.R., Beukes C.W., Chan W.Y., Coetzee M.P., Palmer M., Shapiro N.,
RA Blom J., Stepkowski T., Venter S.N., Steenkamp E.T.;
RT "Genome-informed Bradyrhizobium taxonomy: where to from here?";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00025613}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TAI62471.1}.
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DR EMBL; PSRR01000223; TAI62471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q8QRJ9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000292824; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000292824};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 879 AA; 96583 MW; 513F69A0F0D7B2F4 CRC64;
MNIEKYTERA RGFIQSAQSL AVREGHQQFS PLHLLKVLLD DSEGLAGGLI DRAGGNSRAI
LKATEDALNK LPKVSGSGAG QVYLSPELAR AFDAAEKAAE KAGDSFVTVE RLLLGLALEK
NSEAGSILSK GGVTPQNLNA AIESLRKGRT ADSATAENAY DALKKYARDL TQAARDGKLD
PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAIVEG LALRIVNGDV PESLKDKRLL
SLDLGALIAG AKYRGEFEER LKAVLQEVTS AEGTFILFID EMHTLIGAGK ADGAMDASNL
LKPALARGEL HCIGATTLDE YQKHVEKDAA LARRFQPIFV SEPSVEDTIS ILRGLKDKYE
QHHGVRISDS ALVAAATLSN RYITDRFLPD KAIDLMDEAA ARLKMQVDSK PEELDTLDRE
IIRLKIEQEA LKKESDLGSK SRLQALEKEL ADLEEKSKAL TARWSAEKNK LSNAQKLKAE
LDALRVELAN AQRRGEFQRA GELAYGKIPA LEKQLADIEA SENQGATMEE AVTANHIAQV
VSRWTGVPVD RMLEGEKEKL LKMEDALGRR VVGQAEAVRA VATAVRRSRA GLQDPNRPMG
SFMFLGPTGV GKTELTKALA EYLFNDETAM VRLDMSEYTE KHSVSRLIGA PPGYVGYDEG
GALTEAVRRR PYQVVLFDEI EKAHPDVFNV LLQVLDDGRL TDGQGRTVDF RNTLIIMTSN
LGSEFLVNQP EGEDTDAVRE QVMATVRAHF RPEFLNRVDE IILFHRLQKS EMGRIVEIQF
ARLQKLLEDR KITLTLDAAA RDWLAAKGWD PAYGARPLKR VIQRSLQDPL AEMILAGDIK
DGDQVKISAE GNVLTFNGKA QQTAEVAQFD APVAKRKLN
//
