ID H0PTI4_9RHOO Unreviewed; 859 AA.
AC H0PTI4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
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:BAL24149.1};
GN ORFNames=AZKH_1836 {ECO:0000313|EMBL:BAL24149.1};
OS Azoarcus sp. KH32C.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL24149.1, ECO:0000313|Proteomes:UP000007106};
RN [1] {ECO:0000313|EMBL:BAL24149.1, ECO:0000313|Proteomes:UP000007106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH32C {ECO:0000313|EMBL:BAL24149.1,
RC ECO:0000313|Proteomes:UP000007106};
RA Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA Senoo K.;
RT "Complete genome sequence of Azoarcus sp. KH32C.";
RL Submitted (NOV-2011) 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; AP012304; BAL24149.1; -; Genomic_DNA.
DR RefSeq; WP_015435454.1; NC_020516.1.
DR AlphaFoldDB; H0PTI4; -.
DR STRING; 748247.AZKH_1836; -.
DR KEGG; aza:AZKH_1836; -.
DR PATRIC; fig|748247.4.peg.1787; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000007106; 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:UP000007106};
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 859 AA; 95652 MW; 64CDA81D7D9D6398 CRC64;
MRFDKLTTKF QQALSDAQSI AVGNDQQFIE PAHLLLAMLA QEDGGTVSLL QRAGVNVPPL
KVSLDKLLAR LPKVEGHGGE VQIGRDLSNL LNLADREAQK RGDQFIASEM FLLALADDKG
DTGRTLKEHG LSRKALEAAI EAVRGGAGVA SQDAEGQREA LTKYCIDLTE RARAGKLDPV
IGRDDEIRRA IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNAEVPE TLKGKRVLSL
DMAALLAGAK YRGEFEERLK SVLKEIAQEE GQIIVFIDEI HTMVGAGKAE GAIDAGNMLK
PALSRGELHC IGATTLDEYR KYIEKDAALE RRFQKVLVEE PSVESTIAIL RGLQERYELH
HGVDITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAAAR IKMEIDSKPE VMDKLERRLI
QLKIEQEAVK RETDEASQKR LVLIRDEIEK LEREYANLDE IWRSEKASVQ GSQHIKEEID
KLRAQMAEMQ RKGQYDKLAE LQYGKLPQLE AQLKVAEEAG SGERKFKLLR TQVGTEEIAE
VVSRATGIPV SKMMQGEREK LLRMEERLHS RVVGQDEAVR LVSDAIRRSR AGLSDENRPY
GSFLFLGPTG VGKTELCKAL AEFLFDSEEH LIRVDMSEFM EKHSVARLIG APPGYVGYEE
GGYLTEQVRR KPYSVILFDE VEKAHPDVFN VLLQVLDDGR MTDGQGRTVD FKNTVIVMTS
NLGSQMIQQM SGDDYQVIKL AVMAEVKTFF RPEFVNRIDE VVVFHALDEK HIASIARIQL
QYLERRLARL DMTLQVTDAA LAELAAAGFD PIFGARPLKR AIQEHIENPL ARAILEGQFG
AKDKIVVDSS GGRVAFAKG
//
