ID F7QJ62_9BRAD Unreviewed; 877 AA.
AC F7QJ62;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:EGP08846.1};
GN ORFNames=CSIRO_1598 {ECO:0000313|EMBL:EGP08846.1};
OS Bradyrhizobiaceae bacterium SG-6C.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae.
OX NCBI_TaxID=709797 {ECO:0000313|EMBL:EGP08846.1, ECO:0000313|Proteomes:UP000003148};
RN [1] {ECO:0000313|EMBL:EGP08846.1, ECO:0000313|Proteomes:UP000003148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-6C {ECO:0000313|EMBL:EGP08846.1,
RC ECO:0000313|Proteomes:UP000003148};
RX PubMed=21742875; DOI=10.1128/JB.05647-11;
RA Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G.,
RA Pandey G.;
RT "Genome Sequence of the Newly Isolated Chemolithoautotrophic
RT Bradyrhizobiaceae Strain SG-6C.";
RL J. Bacteriol. 193:5057-5057(2011).
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:EGP08846.1}.
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DR EMBL; AFOF01000017; EGP08846.1; -; Genomic_DNA.
DR AlphaFoldDB; F7QJ62; -.
DR STRING; 709797.CSIRO_1598; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_5; -.
DR Proteomes; UP000003148; 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 COILED 414..501
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 877 AA; 96385 MW; 3524C3F820D2B3DE CRC64;
MNIEKYTDRV KGFIQSAQTL AMREGHQQFT PLHILKVLLD DSEGLAGGLI DRSGGNSRAI
LKATEDALNK MPKVSGAGAG QVYLAPATAR AFDAAEQAAE KAGDSFVTVE RLLQALAADK
DSDAGALLAK GGVTPQNLNA AINALRKGRT ADSASAENAY DALKKYARDL TEAAHDGKLD
PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAIVEG LALRIINGDV PESLKDKKVL
SLDMGALIAG AKYRGEFEER LKAVLSEVTS SDGQIILFID EMHTLVGAGK ADGAMDASNL
LKPALARGEL HCIGATTLDE YRKHVEKDAA LARRFQPVFV SEPTVEDAVS ILRGLKEKYE
LHHGVRITDS AIVSAATLSN RYITDRFLPD KAIDLIDEAA ARLKMQIDSK PEELDNIDRE
IVRLKIEQEA LKKETDSASK DRLQRLEKEL ADLEEKGGAL TAKWQSERDK LSNAQKVKSE
LEQARQELAD AQRRGEFQKA GELAYGRIPE LEKKLKALEE SEKAGNVVLE EAVTSSHVAQ
VVSRWTGIPV DKMLEGEREK LLKMELQLAE RVIGQAEAVG AVSTAVRRSR AGLQDPNRPI
GSFMFLGPTG VGKTELTKAL AEYLFDDETA MVRLDMSEFM EKHSVARLIG APPGYVGYDE
GGVLTEAVRR RPYQVVLFDE IEKAHPDVFN VLLQVLDDGR LTDGQGRTVD FRNTLIIMTS
NLGSEFLVSQ AEGEDTSAVR EQVMAVVRAS FRPEFLNRVD EIILFHRLQR TEMGRIVDIQ
MRRLLKLLAD RKITLTLDEK AREWLAAKGW DPAYGARPLK RAIQRAVQDP LAEMILSGRI
HDGENVVVSA KDEGLTFNGQ LARIDTETPP VPKSKLN
//
