ID A0A0U2XSW6_9BURK Unreviewed; 875 AA.
AC A0A0U2XSW6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=AT302_22575 {ECO:0000313|EMBL:ALS62158.1};
OS Pandoraea norimbergensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=93219 {ECO:0000313|EMBL:ALS62158.1, ECO:0000313|Proteomes:UP000060277};
RN [1] {ECO:0000313|Proteomes:UP000060277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11628 {ECO:0000313|Proteomes:UP000060277};
RA Ee R., Lim Y.-L., Yong D., Yin W.-F., Chan K.-G.;
RT "Complete genome sequence of Pandoraea norimbergensis DSM 11628.";
RL Submitted (DEC-2015) 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; CP013480; ALS62158.1; -; Genomic_DNA.
DR RefSeq; WP_058379023.1; NZ_CP013480.3.
DR AlphaFoldDB; A0A0U2XSW6; -.
DR STRING; 93219.AT302_22575; -.
DR KEGG; pnr:AT302_22575; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000060277; 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..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 875 AA; 96860 MW; E1DBF8E936903756 CRC64;
MRQDKFTTQF LEALADAQSM AVGRDQQYIE PLHLLAALIA QPEGAARSLL QRAGVQVQPL
AHDIETALSK LPQVQGTDGN VQVSRELAGL LNQADKEAQK HGDSYIASEM FLLALADDKG
DTGKLARARG LTRKALEAAI VGVRGGESVN SQDAESQREA LKKYTLDLTE RAALGKLDPV
IGRDDEIRRT IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE SLKNKRVLAL
DMAGLLAGAK FRGEFEERLK SVLNDIAKDE GRTILFIDEI HTMVGAGKAE GAMDAGNMLK
PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVLVEE PSVEATIAIL RGLQEKYELH
HGVEITDPAI VAAAELSQRY ITDRFLPDKA IDLIDEAASK IKMEIDSKPE VMDKLDRRLI
QLKIEREAIK KETDEASQKR LALIEEEISR LEREYADLEE IWTAEKAAVQ GSAQVKEEID
RVRAELAKLQ REGKLDKVAE LQYGKLPQLE AQLKDAAAAE AAGQQAHPRL LRTQVGTEEI
AEVISRATGI PVSKMMQGER EKLLNMEGKL HERVVGQDEA ITAVADAIRR SRAGLSDPDR
PYGSFLFLGP TGVGKTELCK ALAMFLFDSE DHLIRIDMSE FMEKHSVARL IGAPPGYVGY
EEGGYLTEAV RRKPYSVILL DEVEKAHPDV FNVLLQVLDD GRMTDGQGRT VDFKNTVIVM
TSNLGSSMIQ SMVGEPQERI KDAVWLEIKE HFRPEFLNRI DEVVVFHGLD QKHIESIATI
QIEILRKRLA KLDMALEVSK AALMHVAREG FDPVFGARPL KRAIQQEIEN PVAKLVLAGK
FGPKDTIPVD WRNGRFTFDG DTAAQVSKET EAAAE
//
