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Database: UniProt
Entry: A0A1J0WKC2_9RHOB
LinkDB: A0A1J0WKC2_9RHOB
Original site: A0A1J0WKC2_9RHOB 
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
//
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