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
//