ID A0A5J6N4B9_9PROT Unreviewed; 864 AA.
AC A0A5J6N4B9;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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:QEX24277.1};
GN ORFNames=FRZ61_42180 {ECO:0000313|EMBL:QEX24277.1};
OS Hypericibacter adhaerens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Dongiaceae; Hypericibacter.
OX NCBI_TaxID=2602016 {ECO:0000313|EMBL:QEX24277.1, ECO:0000313|Proteomes:UP000325797};
RN [1] {ECO:0000313|EMBL:QEX24277.1, ECO:0000313|Proteomes:UP000325797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R5959 {ECO:0000313|EMBL:QEX24277.1,
RC ECO:0000313|Proteomes:UP000325797};
RA Noviana Z.;
RT "Hyperibacter terrae gen. nov., sp. nov. and Hyperibacter viscosus sp.
RT nov., two new members in the family Rhodospirillaceae isolated from the
RT rhizosphere of Hypericum perforatum.";
RL Submitted (AUG-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}.
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DR EMBL; CP042582; QEX24277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J6N4B9; -.
DR KEGG; hadh:FRZ61_42180; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000325797; 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:UP000325797};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 864 AA; 94967 MW; 26296F2B2263FB6F CRC64;
MELEKFTERV RGFIQSAQGL ALRSGHQRFT PEHLLKVLLD DREGLAANLI RAGGGDPVRA
LKETEAELAK LPKVEGSGAG QVYLAPETAR LFDSATTLAE KAGDSFVTAE RMLQALALAA
GTPSAAILKR LNVTPQALEK AIAELRQGRQ AHSASAEDSY EALKKYARDL TQAARDGKLD
PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAIVEG LALRIVNGDV PESLKNKRLM
ALDLGALVAG AKFRGEFEER LKAVLQEVSA AAGEVILFID ELHTLVGAGA AEGAMDASNM
LKPALARGEL HCVGATTLDE YRKHIEKDAA LARRFQPVLV SQPSVEETIS ILRGLKEKYE
LHHGVRITDG ALVSAATLSN RYITDRFLPD KAIDLVDEAA SRLRMQMDSK PEDIDELDRK
LIQLKIEREA LKKESDRASV ERLKNLEKEI AELEEESAKL TAAWQAEKTQ LAGAQKIKEQ
IDQARAEAEQ AQRRGDLARA GELLYGRIPE LQRQLEKAQQ AEQHRVLNEV VGENEIAEVV
SRWTGVPVDK MLQGERDKLL KMEELLASRV IGQQDAIVAI SNAVRRARAG LQDPNRPIGS
FLFLGPTGVG KTELTKALAA FLFDDEHAMV RIDMSEYMEK HSVSRLIGAP PGYVGYDEGG
ALTEAVRRRP YQVVLFDEVE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFR NTLIVLTSNL
GSDILASQPE GQDSAAVREQ VMEVVRSAFR PEFLNRLDEI LLFHRLTRAQ MTGIVEIQLK
RLVAMLAERR IALELDERAK TWLADAGYDP VYGARPLKRV IQRELQNPLA NLLLAGRIAD
GDTVKVSANA KGLTINGEAV AKAA
//
