ID A0A1J0WKC2_9RHOB Unreviewed; 871 AA.
AC A0A1J0WKC2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BOO69_16150 {ECO:0000313|EMBL:APE44764.1};
OS Sulfitobacter alexandrii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1917485 {ECO:0000313|EMBL:APE44764.1, ECO:0000313|Proteomes:UP000181897};
RN [1] {ECO:0000313|EMBL:APE44764.1, ECO:0000313|Proteomes:UP000181897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM1-D1 {ECO:0000313|EMBL:APE44764.1,
RC ECO:0000313|Proteomes:UP000181897};
RA Yang Q., Zhang X., Tian X.;
RT "Complete genome sequence of Sulfitobacter sp. AM1-D1, a toxic bacteria
RT associated with marine dinoflagellate Alexandrium minutum in East China
RT Sea.";
RL Submitted (NOV-2016) 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|ARBA:ARBA00004496,
CC 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; CP018076; APE44764.1; -; Genomic_DNA.
DR RefSeq; WP_071973109.1; NZ_CP018076.1.
DR AlphaFoldDB; A0A1J0WKC2; -.
DR STRING; 1917485.BOO69_16150; -.
DR KEGG; suam:BOO69_16150; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000181897; 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 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 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..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 95545 MW; 36733731366BB82D CRC64;
MDLSKFTERS RGFVQAAQTI AIRESHQRLA PEHILKALLD DEQGFASNLI LAAGGNARRV
TENLALALGK LPKVTGDAAQ VYLDNTTAKV LAEAEALAKK AGDSFVPVER LLMALCMVKS
PAKTALEAGQ VSAQALNAAI NDVRKGRTAD TASAEDGYEA LKKYSTDLTQ RAEEGRIDPI
IGRDEEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVDGDVPE SLRNKRLLAL
DMGALIAGAK YRGEFEERLK AVLTEVTEAA GEIILFIDEM HTLVGAGKTD GAMDASNLLK
PALARGELHC VGATTLDEYR KYVEKDAALA RRFQPVMVQE PTVEDTVSIL RGIKEKYELH
HGVRISDSAL VAAATLSNRY ITDRFLPDKA IDLMDEAASR LRMEVDSKPE ELDALDRQVL
QLQIEEEALK LEDDQASKDR LATLQKDLSD LQERAAEMTA AWQAERDKLA GARDLKEKLD
RARADLDIAK REGNLAKAGE LSYGVIPQLE KELEAAESRE DGMMVEEAVR PEQIASVVER
WTGVPAGKML EGERDKLLRM EEQLHARVIG QDSAVKAVAN AVRRARAGLN DENRPLGSFL
FLGPTGVGKT ELTKAVAEFL FDDDNAMVRI DMSEFMEKHS VARLIGAPPG YVGYDEGGVL
TEAVRRRPYQ VVLFDEVEKA HPDVFNVLLQ VLDDGVLTDG QGHRVDFKQT LIVLTSNLGA
QALSQLPEGG DMARAKRDVM DAVRAHFRPE FLNRLDETII FDRLSRENMT GIVDVQLQRL
LKRLAGRKIV LDLDEGAKKW LGDEGYDPVF GARPLKRVIQ RTLQDPLAEM ILAGDIRDGD
TITVTAGADG LIIGDRVAAS NRPKPNDATV H
//