ID A0A437JT88_9BURK Unreviewed; 869 AA.
AC A0A437JT88;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:RVT50380.1};
GN ORFNames=ENE75_15290 {ECO:0000313|EMBL:RVT50380.1};
OS Rubrivivax albus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Rubrivivax.
OX NCBI_TaxID=2499835 {ECO:0000313|EMBL:RVT50380.1, ECO:0000313|Proteomes:UP000288178};
RN [1] {ECO:0000313|EMBL:RVT50380.1, ECO:0000313|Proteomes:UP000288178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICH-3 {ECO:0000313|EMBL:RVT50380.1,
RC ECO:0000313|Proteomes:UP000288178};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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:RVT50380.1}.
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DR EMBL; SACT01000005; RVT50380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437JT88; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000288178; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000288178};
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 869 AA; 95774 MW; 70E1095EB38CE46F CRC64;
MRFDKLTTAF QQALGDAQSL AVARDNPYIE PAHLLAAMLQ QPDGPKALLD RAGANTAALK
TAMETAIGGF PSVQVSGGQP VQPSRDLVTL LQAADKEASK RGDQFIASEM FLLAAADAKS
DFGGILRGHG LTRKALEAAI DAVRGGQTVD SAEAEGQREA LKKYTLDLTE RARHGKLDPV
IGRDDEIRRA IQVLQRRSKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPD SLREKRVLVL
DMAGLLAGAK YRGEFEERLK AVLKEVAADE GRIILFIDEI HTMVGAGKAE GAIDAGNMLK
PALARGELHC IGATTLNEYR KYVEKDAALE RRFQKVLVDE PTVEATVAIL RGLQEKYEVH
HGVEITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAAAK IKIEIDSKPE AMDKLDRRLI
QLKIEREAVR KEKDEASIKR MGLIEEEIAK LEREAADLEE IWKSEKAQAQ GSAQVKEEID
RARQQIEELK RKGDFNAVAE LQYGKLPELE KRLHEAQAKE TGKKEAGKDG KAGPQLLRTM
VGAEEIAEVV SRATGIPVSK LMQGERDKLL QMESKLHERV VGQDEAIVAV ADAIRRSRAG
LSDPNRPLGS FLFLGPTGVG KTELCKALAG FLFDSEDHMV RIDMSEFMEK HSVSRLIGAP
PGYVGYDEGG YLTEAVRRKP YSVLLLDEVE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFK
NTVIVMTSNL GSHVIMQMAG QPSEDIKEAV WAEVKQHFRP EFLNRIDETV VFHALDQAHI
ENIAKIQLKH LEQRLAKMEM KLEVSPEALA ELAKAGFDPV FGARPLKRAI QHRIENPVSK
LILQGRFGPK DVIPVDVEGG QFVFERTVH
//