ID A0A347UDF9_9RHOB Unreviewed; 854 AA.
AC A0A347UDF9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:AXX96887.1};
GN ORFNames=BAR1_02425 {ECO:0000313|EMBL:AXX96887.1};
OS Profundibacter amoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Profundibacter.
OX NCBI_TaxID=2171755 {ECO:0000313|EMBL:AXX96887.1, ECO:0000313|Proteomes:UP000261704};
RN [1] {ECO:0000313|EMBL:AXX96887.1, ECO:0000313|Proteomes:UP000261704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAR1 {ECO:0000313|EMBL:AXX96887.1,
RC ECO:0000313|Proteomes:UP000261704};
RA Le Moine Bauer S., Sjoeberg A.G., L'Haridon S., Stokke R., Roalkvam I.,
RA Steen I.H., Dahle H.;
RT "Profundibacter amoris BAR1 gen. nov., sp. nov., a new member of the
RT Roseobacter clade isolated at Lokis Castle Vent Field on the Arctic Mid-
RT Oceanic Ridge.";
RL Submitted (SEP-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}.
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DR EMBL; CP032125; AXX96887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A347UDF9; -.
DR KEGG; pamo:BAR1_02425; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000261704; Chromosome.
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:UP000261704};
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 854 AA; 94100 MW; F5E8B9478201B1AA CRC64;
MDMEKFTERS RGFIQAAQTI AMREDHQKLA PEHLLKALMD DDQGLASNLI RAAGGAPERV
VEAVDAALEK LPKVTGDTGQ VYLDSQTAKV LDEAQKIAKK AGDSFVPVER ILMALAMVKS
KAKDALDAGA VTAQKLNEAI NDVRKGRTAD TATAEEGYDA LKKYAIDLTE RAAEGKIDPI
IGRDEEIRRT MQVLSRRTKN NPVLIGEPGV GKTAIVEGLA LRIINGDVPE SLQDKKLLSL
DMGSLIAGAK YRGEFEERLK AVLNEVTSAA GEIILFIDEM HTLIGAGKGD GAMDASNLLK
PALARGELHC VGATTLDEYR KHVEKDAALA RRFQPVLVEE PTVEDTISIL RGIKEKYELH
HGVRISDAAL VAAATLSHRY ITDRFLPDKA IDLMDEAASR LRMEVDSKPE ELDALDREIM
QKQIEAEALK KEDDAASKDR LETLEKELAE LMERSAEMTA KWQAERAKLA SVRELKEQLE
QARAELEIAK REGDLTRAGE LSYSVIPGLE AKLKEAEQRE SDVMVEEAVR PEQIAQVVER
WTGIPTSKML EGERDKLLKM EEEIGKRVIG QKQAVTAVAN SVRRARAGLN DPNRPLGSFL
FLGPTGVGKT ELTKALAEYL FDDEHAMVRI DMSEFMEKHS VARLIGAPPG YVGYDEGGVL
TEAVRRKPYQ VILFDEVEKA HPDVFNVLLQ VLDDGVLTDG QGRTVDFKQT LIILTSNLGS
QALSELPEGS DASEAKDQVM EAVRAHFRPE FLNRLDEIVI FDRLAREDMT GIVDIQLGLL
AKRLAVRKIA LEVDDAAKKW LGDKGYDPVY GARPLKRVIQ HYLQDPLAEK LLAGEVLDGA
TVKVTANEDG LVIS
//
