ID A0A231HL56_9BURK Unreviewed; 866 AA.
AC A0A231HL56;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:OXR49614.1};
GN ORFNames=PuT2_07465 {ECO:0000313|EMBL:OXR49614.1};
OS Pusillimonas sp. T2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pusillimonas.
OX NCBI_TaxID=1548123 {ECO:0000313|EMBL:OXR49614.1, ECO:0000313|Proteomes:UP000216496};
RN [1] {ECO:0000313|EMBL:OXR49614.1, ECO:0000313|Proteomes:UP000216496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T2 {ECO:0000313|EMBL:OXR49614.1,
RC ECO:0000313|Proteomes:UP000216496};
RA Yuan M., Qiu J.G., Ma Y.;
RT "The genome sequence of Pusillimonas sp. T2.";
RL Submitted (JUN-2017) 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:OXR49614.1}.
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DR EMBL; NIQA01000003; OXR49614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A231HL56; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000216496; 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:UP000216496};
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"
FT COILED 778..805
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 866 AA; 96130 MW; 536AB1A4E4070218 CRC64;
MRFDKLTTKF QQAIADAQSL AVQNDNQYIE PVHVLAALLA DTDSGTGSLL ARAGVATSRL
TSSLNTAIKA LPQVKGAGGN VQVGRELQAA LARTDKEASN RGDTYIASEL FLLALVDDKG
EAGRLLREAG LQRKPLEAAV EAVRGGATVS DAEGESNREA LKKYTTDLTE RAREGKLDPV
IGRDDEIRRA IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINNEVPE TLKGKRVLSL
DLAALLAGAK YRGEFEERLK AVLKELSQDQ GGIIVFIDEI HTMVGAGKAE GAMDAGNMLK
PALSRGELHC IGATTLDEYR KYIEKDAALE RRFQKVLVNE PDVESTIAIL RGLQERYELH
HGVAITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAAAR IRMEIDSKPE VMDKLDRRII
QLKIEREAVK KETDEGSLRR LKAIEDELEK LQREYNDYEE IWKAEKAAVQ GSQSVKEEIE
RTRAEMAELQ RKGQFDKLAE LQYGKLPELE ARLKAAEASG DGDKTAETDK PRLLRTQVGA
EEIAEVVARA TGIPVSKMMQ GERAKLLGME DHLHRRVVGQ DEAVSLVADA IRRSRAGLSD
PSRPYGSFLF LGPTGVGKTE LTKALADFLF DSEEHLIRID MSEFMEKHSV ARLIGAPPGY
VGYEEGGYLT EAVRRKPYSV ILLDEVEKAH PDVFNVLLQV LDDGRLTDGQ GRTVDFRNTV
VVMTSNLGSQ HIQSMAGQPY EVIKEVVWEE LKTSFRPEFL NRIDEVVVFH GLDAKHIESI
AKIQIQRLQQ RLAQQEMRLE VSDAALAQLA RTGFDPVFGA RPLKRAIQQH IENPVARLLL
EGKFGPKDVI PVDWQDDKFV FERTLQ
//