ID A0A2U8GNA3_9RHOO Unreviewed; 860 AA.
AC A0A2U8GNA3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:AWI74980.1};
GN ORFNames=CEW83_06870 {ECO:0000313|EMBL:AWI74980.1};
OS Parazoarcus communis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Parazoarcus.
OX NCBI_TaxID=41977 {ECO:0000313|EMBL:AWI74980.1, ECO:0000313|Proteomes:UP000244930};
RN [1] {ECO:0000313|EMBL:AWI74980.1, ECO:0000313|Proteomes:UP000244930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSPY31 {ECO:0000313|EMBL:AWI74980.1,
RC ECO:0000313|Proteomes:UP000244930};
RA Woo J.-H., Kim H.-S.;
RT "Azoarcus.";
RL Submitted (JUN-2017) 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; CP022187; AWI74980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U8GNA3; -.
DR KEGG; acom:CEW83_06870; -.
DR Proteomes; UP000244930; 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 Reference proteome {ECO:0000313|Proteomes:UP000244930};
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; 95730 MW; 9CAD3644D608AA48 CRC64;
MRFDKLTTKF QQALNDAQSI ALGNDQQFIE PQHLLLAMLG QDDGGTVSLL QRAGVNVPPL
KAALQKALER LPKVEGHGGE VQVGRDLSNL LNLTDKEAQK RGDQFIASEM FLLALSNDKG
ETGRLMKEHG LSRKPLEAAI EAVRGGASVG SQDAEAQRES LAKYCLDLTE RARSGKLDPV
IGRDDEIRRA IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE TLKGKKVLSL
DMAALLAGAK YRGEFEERLK AVLKEIAQEE GQVILFIDEI HTMVGAGKAE GAMDAGNMLK
PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVQVDE PTVEATIAIL RGLQEKYEIH
HGVDITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAGAR IKMEIDSKPE VMDKLDRRMI
QLKIEREAVK KEKDEASKKR LQLIEDELAK LQREYNDLEE VWKAEKSRAS GSAHIKEEID
QLRAQMADFQ RKGQLDKVAE LQYGKLPQLE AQLKMAEQAG ENATPNKLLR TQVGAEEIAE
VVSRATGIPV SKMMQGEREK LLKMEERLHA RVVGQDEAVH LVSDAIRRSR AGLSDENRPY
GSFLFLGPTG VGKTELCKSL AEFLFDSEEH LVRIDMSEFM EKHSVARLIG APPGYVGYEE
GGYLTEQVRR KPYSVILFDE VEKAHPDVFN VLLQVLDDGR MTDGQGRTVD FKNTVIVMTS
NLGSQMIQQM AGSDYGVVKL AVMAEVKTFF RPEFINRIDE VVVFHSLDEK NIAGIAKIQL
QYLEKRLARL EMKLEVSDAA LADIASAGFD PVFGARPLKR AIQERIENPL ARAILEGQFG
AEDRIRADIE NGQIVFSRMQ
//