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Database: UniProt
Entry: W0SGW0_9PROT
LinkDB: W0SGW0_9PROT
Original site: W0SGW0_9PROT 
ID   W0SGW0_9PROT            Unreviewed;       864 AA.
AC   W0SGW0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB1 {ECO:0000313|EMBL:BAO30261.1};
GN   Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SUTH_02478 {ECO:0000313|EMBL:BAO30261.1};
OS   Sulfuritalea hydrogenivorans sk43H.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Sterolibacteriaceae; Sulfuritalea.
OX   NCBI_TaxID=1223802 {ECO:0000313|EMBL:BAO30261.1, ECO:0000313|Proteomes:UP000031637};
RN   [1] {ECO:0000313|EMBL:BAO30261.1, ECO:0000313|Proteomes:UP000031637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM22779 {ECO:0000313|EMBL:BAO30261.1};
RX   PubMed=25017294; DOI=10.1016/j.syapm.2014.05.010;
RA   Watanabe T., Kojima H., Fukui M.;
RT   "Complete genomes of freshwater sulfur oxidizers Sulfuricella denitrificans
RT   skB26 and Sulfuritalea hydrogenivorans sk43H: genetic insights into the
RT   sulfur oxidation pathway of betaproteobacteria.";
RL   Syst. Appl. Microbiol. 37:387-395(2014).
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; AP012547; BAO30261.1; -; Genomic_DNA.
DR   RefSeq; WP_041099619.1; NZ_AP012547.1.
DR   AlphaFoldDB; W0SGW0; -.
DR   STRING; 1223802.SUTH_02478; -.
DR   KEGG; shd:SUTH_02478; -.
DR   HOGENOM; CLU_005070_4_0_4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000031637; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:BAO30261.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:BAO30261.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031637};
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   864 AA;  95290 MW;  00870FE921F8E4E6 CRC64;
     MRFDKFTTKF QQAVSDAQSL AVGNDQQFIE PLHLLLALLN QEDGGTASLL ARAGANVGGL
     KAQLAKAMER LPRVEGHGGE VSIGRDLANL LNVTDKEAQK AGDQFIASEM FLLALTQDKG
     EAGRLLKEAG LNRKALEDAV KAVRGGESVG SQEAEGQREA LNKYCLDLTE RARLGKLDPV
     IGRDDEIRRS IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE TLKNKRVLVL
     DMAGLLAGAK YRGEFEERLK AVLKEVALDE GRIILFIDEL HTMVGAGKAE GAIDAGNMLK
     PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVQVDE PSVEATIAIL RGLQEKYELH
     HGVDITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAAAK IKMEIDSKPE VMDKLDRRLI
     QLKIESEAVK KEKDEASQKR LVLIKDEMDK LERELANLDE IWRAEKAQVQ GSAHVKEEID
     KLKVQMAELQ RKGAFDKLAE LQYGQLPKLE AQLKAADSAA SGVGAGGTAK NRLLRTQVGT
     EEIAEVVSRA TGIPVSKMMQ GERDKLLKME DKLHGRVVGQ DEAVRLVSDA IRRSRAGLSE
     ESRPYGSFLF LGPTGVGKTE LCKALAEFLF DAEDHLIRID MSEFMEKHSV ARLIGAPPGY
     VGYEEGGHLT EQVRRKPYSV ILFDEVEKAH PDVFNVLLQV LDDGRMTDGQ GRTVDFKNTV
     IVMTSNLGSQ MIQQMSGSDY QVVKMAVMGE VKTHFRPEFV NRIDEIVVFH ALDEKNIAGI
     ARIQLKYLEK RMAKLDMTLE VSDAALALLA EAGFDPVFGA RPLKRAIQER IENPLSRLIL
     DGSFGAKDNV KVEVAKGTLS FNKA
//
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