ID A0A4R2P0F6_RHOAD Unreviewed; 871 AA.
AC A0A4R2P0F6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=EV656_1017 {ECO:0000313|EMBL:TCP27105.1};
OS Rhodovulum adriaticum (Rhodopseudomonas adriatica).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=35804 {ECO:0000313|EMBL:TCP27105.1, ECO:0000313|Proteomes:UP000295733};
RN [1] {ECO:0000313|EMBL:TCP27105.1, ECO:0000313|Proteomes:UP000295733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2781 {ECO:0000313|EMBL:TCP27105.1,
RC ECO:0000313|Proteomes:UP000295733};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-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:TCP27105.1}.
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DR EMBL; SLXL01000001; TCP27105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R2P0F6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000295733; 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 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 Hydrolase {ECO:0000313|EMBL:TCP27105.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TCP27105.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295733};
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..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 95687 MW; EB6804FF65074C45 CRC64;
MNLEKFTERS RGFLQAAQTI AMRESHQRLA PEHLLKALMD DEEGMASNLI RRAGGAPERV
VDAVDAALAK MPKVSGDAGQ TYLDQTTGRV LDEAEKIATK AGDSYVPVER ILMALAMVKS
RAKDALDAGA VTAQNLNAAI NDIRKGRTAD TASAEQGYDA LKKYARDLTE MAEEGKIDPI
IGRDEEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE SLKNKRLMAL
DMGALIAGAK YRGEFEERLK AILSEITAAA GEIILFIDEM HTLVGAGKSE GAMDAANLIK
PALARGELHC IGATTLDEYR KHVEKDAALA RRFQPLMVEE PTVEDTVSIL RGIKEKYELH
HGVRISDAAL VSAATLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDALDRDIL
QKQIEAEALR KEDDAASKDR LAKLEQELAD LQQKSASMTA KWQAERDKLE GARDLKEKLD
RARAELDHAK REGDLAKAGE LSYGVIPQLE KQLAEAEAQD DDVMVEEAVR PEQIAQVVER
WTGIPTSKML EGEREKLLRM EEELGKRVIG QKAAVTAVAN AVRRARAGLN DENRPLGSFL
FLGPTGVGKT ELTKAVAEYL FDDDQAMVRI DMSEFMEKHS VARLIGAPPG YVGYDEGGVL
TEAVRRRPYQ VVLFDEVEKA HPEVFNVLLQ VLDDGVLTDG QGRTVDFKQT LIVLTSNLGS
QALSQLPEDG DASAAKRDVM DAVRAHFRPE FLNRLDEMVV FDRLTRADMT GIVEIQLSRL
EKRLAGRNIT LELDESARKW LADAGYDPVY GARPLKRVIQ RSLQDRLAEM ILGGEIRDGQ
TVPVHAGADG LIVGDRVGGS DRPAPGDAVV H
//
