ID A0A2V1K140_9BURK Unreviewed; 866 AA.
AC A0A2V1K140;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:PWF24158.1};
GN ORFNames=DD235_07650 {ECO:0000313|EMBL:PWF24158.1};
OS Corticimicrobacter populi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Corticimicrobacter.
OX NCBI_TaxID=2175229 {ECO:0000313|EMBL:PWF24158.1, ECO:0000313|Proteomes:UP000245212};
RN [1] {ECO:0000313|Proteomes:UP000245212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3d-2-2 {ECO:0000313|Proteomes:UP000245212};
RA Li Y.;
RL Submitted (MAY-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:PWF24158.1}.
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DR EMBL; QETA01000002; PWF24158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1K140; -.
DR Proteomes; UP000245212; 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:UP000245212};
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 866 AA; 96131 MW; BC692EDE9ECDE124 CRC64;
MRFDRFTTKF QQALADAQSL AVRNDHPYIE PVHVLSALLA DTDSGAGSLL ARAGVAVNRV
GAALDGALKA LPQVQGGDGN VQVGRDLQAV LARTDKEAAK RGDTYIASEL FLLALADDKG
EAGRILRDAG LQRAPLEAAI EAVRGGASVQ DAEGEANREA LGKYTLDLTA RAREGKLDPV
IGRDDEIRRA IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNNEVPE TLKNKRVLSL
DLAALLAGAK FRGEFEERLK SVLKELAQEA GNCIVFIDEI HTMVGAGKAE GAMDAGNMLK
PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVLVGE PDVESTIAIL RGLQERYELH
HGVQITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAAAR IRMEIDSKPE VMDRLDRRII
QLKIEREAVR KETDEASLRR LKAIEDELES LQREYNDYEE IWKAEKAAVQ GTQAIKEEIE
RLRAEMAEAQ RKGQFDKLAE LQYGQLPELE ARLRTAEGSE KAASEGGSER PRLLRTQVGT
EEIAEVVSRA TGIPVAKMMQ GERTKLLEME SFLHKRVVGQ DEAVRLVSDA IRRSRSGLSD
PNRPYGSFLF LGPTGVGKTE LTKALAEFLF DAEDHLIRID MSEFMEKHSV ARLIGAPPGY
VGYEEGGYLT EAVRRKPYSV VLLDEVEKAH PDVFNVLLQV LDDGRLTDGQ GRTVDFRNTV
IVMTSNLGSQ QIQSMANQPY EAVKAVVWDE LKQAFRPEFL NRIDEVVVFH ALDSKNIESI
ARIQLQRLAQ RLQKMDMELD VSEAALAQIA KAGFDPVFGA RPLKRAIQQH IENPVARLIL
EGRFGPRDVV PVDWRDEQFV FSRVLQ
//