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Database: UniProt
Entry: A0A3D8JQH0_9BURK
LinkDB: A0A3D8JQH0_9BURK
Original site: A0A3D8JQH0_9BURK 
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
//
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