ID A0A3D8JQH0_9BURK Unreviewed; 865 AA.
AC A0A3D8JQH0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-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:RDU95349.1};
GN ORFNames=DWV00_29335 {ECO:0000313|EMBL:RDU95349.1};
OS Trinickia dinghuensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=2291023 {ECO:0000313|EMBL:RDU95349.1, ECO:0000313|Proteomes:UP000256838};
RN [1] {ECO:0000313|EMBL:RDU95349.1, ECO:0000313|Proteomes:UP000256838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOM06 {ECO:0000313|EMBL:RDU95349.1,
RC ECO:0000313|Proteomes:UP000256838};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. DHOM06 isolated from forest soil.";
RL Submitted (AUG-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:RDU95349.1}.
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DR EMBL; QRGA01000020; RDU95349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8JQH0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000256838; 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 104; 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:UP000256838};
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 865 AA; 96307 MW; 13359247D2555BC2 CRC64;
MRIDKLTTKF QEALADAQSL AVGRGQQYIE PVHVLSALVA QQDGSARSLL SRAGVHVQAL
QTALNEAISR LPQVQGTDGN VQISRELNGL LNQADKEAQQ LNDTFIASEM FLLACADDKG
EVGRLARQYG LARKSLESAI AAVRGGGQVH SADAESQREA LKKYTIDLTE RARAGKLDPV
IGRDDEIRRS IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE SLKSKRVLSL
DMAGLLAGAK YRGEFEERLK AVLHDIAKDE GQTIVFIDEI HTMVGAGKAE GAMDAGNMLK
PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVLVDE PSVEASIAIL RGLQEKYELH
HGVEITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAASK IKMEIDSKPE EMDRLDRRLI
QLKIEREAVK KEKDEASQKR LQLIEEEIER LNREYSDLEE IWTAEKAAVQ GSAQLKEEIE
KTRAEIVRLQ REGKLEKVAE LQYGKLPELE ARLKQVTQAE ATEQHNPTHR RLLRTQVGAE
EIAEVVSRAT GIPVSRMMQG EREKLLQIES KLHERVVGQE EAIAAVADSI RRSRAGLSDP
NRPYGSFLFL GPTGVGKTEL CKALASFLFD SEEHLIRIDM SEFMEKHSVA RLIGAPPGYI
GYEEGGYLTE AVRRKPYSVI LLDEVEKAHP DVFNVLLQVL DDGRMTDGQG RTVDFKNTVI
VMTSNLGSQM IQSMTDAPQE AVRDAVWTEV KEHFRPEFLN RIDEVVVFHS LDRANIESIA
KIQLQRLHER LAKLDMQLVV SDAALEQIAQ AGYDPLFGAR PLKRAIQQEI ENPVAKLILA
GRFGPKDVIP VEVEGGKLVF ERVVH
//