ID A0A1E1F7P3_9SPHN Unreviewed; 869 AA.
AC A0A1E1F7P3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SCLO_2002060 {ECO:0000313|EMBL:BAV66539.1};
OS Sphingobium cloacae.
OG Plasmid psclo_2 dna {ECO:0000313|Proteomes:UP000218272}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=120107 {ECO:0000313|EMBL:BAV66539.1, ECO:0000313|Proteomes:UP000218272};
RN [1] {ECO:0000313|EMBL:BAV66539.1, ECO:0000313|Proteomes:UP000218272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10874 {ECO:0000313|EMBL:BAV66539.1,
RC ECO:0000313|Proteomes:UP000218272};
RC PLASMID=psclo_2 dna {ECO:0000313|Proteomes:UP000218272};
RA Ootsuka M., Nishizawa T., Ohta H.;
RT "Complete Genome Sequence of the Nonylphenol-Degrading Bacterium
RT Sphingobium cloacae JCM 10874T.";
RL Submitted (OCT-2016) 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; AP017656; BAV66539.1; -; Genomic_DNA.
DR RefSeq; WP_066516355.1; NZ_AP017656.1.
DR AlphaFoldDB; A0A1E1F7P3; -.
DR KEGG; sclo:SCLO_2002060; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000218272; Plasmid psclo_2 dna.
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}; Plasmid {ECO:0000313|EMBL:BAV66539.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218272};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 844..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 415..495
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COMPBIAS 848..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 95398 MW; F9296E56ADA6113E CRC64;
MNLEKYTDRA KGFLQSAQTV AIRLNHQRIT PEHILKALLE DEQGMAAGLI RAAGGNPDLA
TGEVDAALAK LPSVTGSGAS QPPGLDNDAV RLLDQAEQIA QKAGDSYVTV ERLLLALTLA
TGAAAGKALA RAGVKAEALN EAINQLRGGR AADTASAEDR YDALKKFARD LTQAARDGKL
DPVIGRDEEI RRTVQILARR TKNNPVLIGD PGVGKTAIVE GLALRIANGD VPDTLKDRKL
MALDMGALIA GAKYRGEFEE RLKGVLDEVK GAEGDIILFI DEMHTLIGAG KTEGAMDAGN
LLKPALARGE LHCIGATTLD EYRKYVEKDA ALQRRFQPVF VGEPTVEDTV SILRGLKEKY
ELHHGVRITD GAIVAAATLS NRYITDRFLP DKAIDLMDEA ASRIRMEVES KPEEIETLDR
RIIQLKIERE ALRKESDAAS KDRLTHLEHD LAQLEQQSAE LTQRWQAERE KIQAEAKLKE
QLDQARLELD QAQRRGDLAR AGELSYGVIP GLEKQLADAQ TASQGAMLRE EVTAQDIAAV
VSRWTGIPVD KMLEGEREKL LHMEEALGRR VIGQRQAVTA VSRAIRRARA GLQDPDRPMG
SFLFLGPTGV GKTELTKALA GFLFDDDSAM VRIDMSEFME KHSVARLIGA PPGYVGYEEG
GVLTEAVRRR PYQVILFDEV EKAHNDVFNV LLQVLDDGRL TDGQGRTVDF KNTLIILTSN
LGSQYLSNLA EGETVESVEP QVMEVVRAHF RPEFLNRLDE IILFHRLGQA DMGPIVDIQV
ARVQNLLKDR KITLDLTDRA RAWLGRVGYD PVYGARPLKR AIQRYLQDPL ADLLLRGEVP
DGSTVTVDEG DSELTFSTQV SRPAEAQAA
//
