ID A0A4S4AU27_9RHOO Unreviewed; 860 AA.
AC A0A4S4AU27;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:THF63396.1};
GN ORFNames=E6O51_04870 {ECO:0000313|EMBL:THF63396.1};
OS Pseudothauera rhizosphaerae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Pseudothauera.
OX NCBI_TaxID=2565932 {ECO:0000313|EMBL:THF63396.1, ECO:0000313|Proteomes:UP000307956};
RN [1] {ECO:0000313|EMBL:THF63396.1, ECO:0000313|Proteomes:UP000307956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-YHH848 {ECO:0000313|EMBL:THF63396.1,
RC ECO:0000313|Proteomes:UP000307956};
RA Lin S.-Y., Hameed A., Hsu Y.-H., Young C.-C.;
RT "Azoarcus rhizosphaerae sp. nov. isolated from rhizosphere of Ficus
RT religiosa.";
RL Submitted (APR-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:THF63396.1}.
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DR EMBL; SSOD01000003; THF63396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4S4AU27; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000307956; Unassembled WGS sequence.
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:UP000307956};
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 860 AA; 95904 MW; BCE4188E0BE900E8 CRC64;
MRFDKLTTKF QQALADAQSI AVGNDQQFIE PQHLLAAMLD QEDGGTVSLL QRAGVNVPPL
KNTLHKALDR LPRVEGHGGE VQIGRDLNNL LNLTDREAQK RGDQFIASEM FLLALADDKG
EAGRLLKEHG LARKALEAAV DAVRGGQNVG SQDAEGQREA LSKYCLDLTE RARQGKLDPV
IGRDDEIRRA IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNDEVPE TLKGKRVLSL
DMAALLAGAK YRGEFEERLK AVLKDIAQEE GRIIVFIDEI HTMVGAGKAE GAIDAGNMLK
PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVLVDE PSVESTIAIL RGLQEKYEVH
HGVDITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAAAR IKMEIDSKPE SMDKLERRLI
QLKIEQEAVK KETDEASQKR LLLIRDEIGK LEREYANLDE IWRAEKASVQ GSQHIKEEIE
KLRAQMAEMQ RKGQFDKLAE LQYGKLPQLE AQLKAAETAG SGERQFKLLR TQVGAEEIAE
VVSRATGIPV SKMMQGERDK LLHMEERLHA RVVGQDEAVR LVSDAIRRSR AGLADENRPY
GSFLFLGPTG VGKTELCKTL AEFLFDSEEH LIRIDMSEFM EKHSVARLIG APPGYVGYEE
GGYLTEQVRR KPYSVILFDE VEKAHPDVFN VLLQVLDDGR MTDGQGRTVD FKNTVIVMTS
NLGSQMIQQM SGDDYQVIKL AVMAEVKTFF RPEFINRIDE VVVFHALDEK NIAGIARIQL
KYLEKRLARL EMSMEVSDAA LAEIASAGFD PVFGARPLKR AIQERIENPL AKAILEGQFA
AKDRIRVDAA GSKLSFARVE
//
