ID Q131C5_RHOPS Unreviewed; 879 AA.
AC Q131C5;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=RPD_4095 {ECO:0000313|EMBL:ABE41314.1};
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE41314.1, ECO:0000313|Proteomes:UP000001818};
RN [1] {ECO:0000313|EMBL:ABE41314.1, ECO:0000313|Proteomes:UP000001818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE41314.1,
RC ECO:0000313|Proteomes:UP000001818};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) 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}.
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DR EMBL; CP000283; ABE41314.1; -; Genomic_DNA.
DR AlphaFoldDB; Q131C5; -.
DR STRING; 316057.RPD_4095; -.
DR KEGG; rpd:RPD_4095; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_5; -.
DR BioCyc; RPAL316057:RPD_RS20605-MONOMER; -.
DR Proteomes; UP000001818; Chromosome.
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 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 REGION 857..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 879 AA; 96684 MW; 06DF2A7153095609 CRC64;
MNIEKYTERV RGFIQSAQSL AVREGHQQFS PLHILKVLLD DSEGLAGGLI DRAGGNSRAI
LQSTEAALSK MPKVSGSGAG QVYLAPATAR AFDAAEQAAE KAGDSFVTVE RLLLALALDR
ESDAGQLLAK GGVTPQNLNS AINALRKGRT ADSATAENAY DALKKYSRDL TQAARDGKLD
PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAIVEG LALRILNGDV PESLKDKKLL
SLDLGALIAG AKYRGEFEER LKAVLSEVTS AEGGIILFID EMHTLIGAGK ADGAMDASNL
LKPALARGEL HCIGATTLDE YRKHVEKDAA LARRFQPIFV SEPTVEDTVS ILRGLKDKYE
QHHGVRISDS ALVAAVTLSN RYITDRFLPD KAIDLMDEAA ARLKMQVDSK PEELDSMDRE
IVRLKIEQEA LKKETDTGSR TRLVTLEKEL ADLEEKSAAL TARWSAEKNK LSDAQKLKSE
LDGLRLELAD AQRRGEYQRA GELAYGRIPE LEKKLADIEA NENAGEMMEE AVTANHIAQV
VSRWTGVPVD KMLEGEKEKL LRMEDQIGKR VVGQFEAVHA VSTAVRRARA GLQDPNRPMG
SFMFLGPTGV GKTELTKALA QYLFDDETAM VRLDMSEYME KHSVSRLIGA PPGYVGYDEG
GALTEAVRRR PYQVVLFDEI EKAHPDVFNV LLQVLDDGRL TDGQGRTVDF RNTLIVMTSN
LGSEYLVNQP EGEDTEVVRE QVIGMVRGHF RPEFLNRVDE IILFHRLQKT EMGRIVDIQL
GRLAKLLEDR KIVLDLDPAA RDWLAEKGWD PAYGARPLKR VIQRHVQDPL AEMILDGTVK
DGDQVAISTE GGALTFNGQP PHGADIAPFT GRPPKRMLN
//
