ID A0A1V1PME3_9PROT Unreviewed; 863 AA.
AC A0A1V1PME3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=U91I_01262 {ECO:0000313|EMBL:GAM97635.1};
OS alpha proteobacterium U9-1i.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1605283 {ECO:0000313|EMBL:GAM97635.1, ECO:0000313|Proteomes:UP000188260};
RN [1] {ECO:0000313|EMBL:GAM97635.1, ECO:0000313|Proteomes:UP000188260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U9-1i {ECO:0000313|EMBL:GAM97635.1,
RC ECO:0000313|Proteomes:UP000188260};
RA Okano K., Furuta S., Ichise S., Miyata N.;
RT "Whole-Genome Sequences of Two Manganese(II)-Oxidizing Bacteria, Bosea sp.
RT Strain BIWAKO-01 and Alphaproteobacterium Strain U9-1i.";
RL Genome Announc. 4:e01309-16(2016).
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:GAM97635.1}.
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DR EMBL; BBSY01000002; GAM97635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1PME3; -.
DR STRING; 1605283.U91I_01262; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000188260; 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:UP000188260};
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..499
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 94550 MW; 3853552C1B332A6F CRC64;
MDMEKLTDRA KGFVQAAQTI ALREQNQQLE TQHLLKALLD DREGLAAGLI TAAGGDARAV
GAAADAAVQA LPKVQGGGDR MYAASSFARA LDAADQAATK AGDSYVTAER LLFGLAIAEG
KASDVLKKAG VTPQKLEAAI QQLRKGRAAH SSGAEDQYDA LKKYARDLTE DARKGKLDPV
IGRDEEIRRT IQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE GLKNKKLLAL
DMGSLVAGAK YRGEFEERLK AVLNEVTAAE GSIILFIDEM HTLVGAGKSE GAMDASNLLK
PALARGELHC VGATTLDEYR KHVEKDAALA RRFQPVFVNE PTVEDTISIL RGLKEKYEVH
HGVRISDAAI VASAQLSNRY ITDRFLPDKA IDLMDEAASR LRMQVDSKPE ALDELDRRLL
QLKIEVEALK KEKDPASQDR AKKVEAEIGE LETKSAELTS AWSAEKQKLQ IGAKAKEELE
KLQNEYENAV RRGDLARASE LKYGRIPQLE KQIADGEKQA SNSGLVKEVV DAEAIAGVVS
RWTGVPVEKM LEGEKAKLLD METQLRGRVI GQEQALAAVS DAVRRARAGL QDPNRPIGSF
MFLGPTGVGK TELTKALAEF LFDDEHAMTR VDMSEYMEKH AVARLIGAPP GYVGYEEGGA
LTEAVRRRPY QVILFDEVEK AHPDVFNVLL QVLDDGRLTD GQGRTVDFKN TILIMTSNSG
AHFLAELPDG ADADDARDQV MAELRLRFRP EFLNRVDEII LFRRLERAQM GLIVDVQLKR
LVKLLAAREI GIDLDQRAKA ELAKRGYDPA WGARPLKRVI QKDIQDPMAR LILEGRIKDG
DHVGVSFDGN DFLFNGRADR QAA
//
