ID A0A2W7NI60_9RHOB Unreviewed; 871 AA.
AC A0A2W7NI60;
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 ORFNames=LX81_00006 {ECO:0000313|EMBL:PZX19550.1};
OS Palleronia aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Palleronia.
OX NCBI_TaxID=568105 {ECO:0000313|EMBL:PZX19550.1, ECO:0000313|Proteomes:UP000248916};
RN [1] {ECO:0000313|EMBL:PZX19550.1, ECO:0000313|Proteomes:UP000248916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22009 {ECO:0000313|EMBL:PZX19550.1,
RC ECO:0000313|Proteomes:UP000248916};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-2018) 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|ARBA:ARBA00004496,
CC 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:PZX19550.1}.
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DR EMBL; QKZL01000001; PZX19550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7NI60; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000248916; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:PZX19550.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PZX19550.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248916};
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 871 AA; 95876 MW; CDB5454D7A8C3197 CRC64;
MNMEKFTERS RGFIQAAQTI ALRESHQRLT PEHLLKALLD DDQGLASNLI DRAGGNARRV
AEHLALALAK LPKVSGDGSQ TYLDATTGKV LAEAEALAKK AGDSFVPVER ILCALAMVKS
KAKDALDQGG VNAQSLNAAI NDIRKGRTAD SASAEDQYEA LKKFSLDLTE RAREGKIDPI
IGRDDEIRRT MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE SLRDKRLLAL
DMGALIAGAK YRGEFEERLK GVLSEVTAAA GEIVLFIDEM HTLVGAGKAD GAMDASNLLK
PALARGELHC VGATTLDEYR KHVEKDAALA RRFQPLLVEE PTVTDTISIL RGIKEKYELH
HGVRISDSAL VAAATLSHRY ITDRFLPDKA IDLMDEAASR LRMEVDSKPE ELDALDRDIL
QKQIEAEALR KEDDQPSKDR LERLEQELGD LQEQADAMTA QWQSERDKLD ASRILKERLD
RARAELDIAK REGNLARAGE LSYGIIPGLE KELGEAEDRD GDVMVEEAVR PEQIAQVVER
WTGIPTSKML EGEREKLLKM EAELGRRVIG QRTAVTAVAN AVRRARAGLN DENRPLGSFL
FLGPTGVGKT ELTKAVAEYL FDDDQAMVRI DMSEFMEKHA VARLIGAPPG YVGYDEGGVL
TEAVRRRPYQ VILFDEVEKA HPDVFNVLLQ VLDDGVLTDG QGRHVDFKQT LIVLTSNLGS
QALSQLPEGG DAARARRDVM DAVRAHFRPE FLNRLDETVI FDRLSREDMD GIVEIQLRRL
EARLAGRKIV LDLDEGARKW LADEGYDPVF GARPLKRVIQ RALQDQLAEM ILAGDVADGD
TIPVSAGSEG LIVGDRVASS NRHPPEHAVV H
//