ID A0A0D6B6U8_RHOSU Unreviewed; 871 AA.
AC A0A0D6B6U8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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:BAQ70822.1};
GN ORFNames=NHU_03696 {ECO:0000313|EMBL:BAQ70822.1};
OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=35806 {ECO:0000313|EMBL:BAQ70822.1, ECO:0000313|Proteomes:UP000064912};
RN [1] {ECO:0000313|EMBL:BAQ70822.1, ECO:0000313|Proteomes:UP000064912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2351 {ECO:0000313|EMBL:BAQ70822.1,
RC ECO:0000313|Proteomes:UP000064912};
RA Nagao N.;
RT "Genome sequene of Rhodovulum sulfidophilum DSM 2351.";
RL Submitted (FEB-2015) 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; AP014800; BAQ70822.1; -; Genomic_DNA.
DR RefSeq; WP_060835914.1; NZ_AP014800.1.
DR AlphaFoldDB; A0A0D6B6U8; -.
DR KEGG; rsu:NHU_03696; -.
DR PATRIC; fig|35806.4.peg.3790; -.
DR eggNOG; COG0542; Bacteria.
DR Proteomes; UP000064912; 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 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 871 AA; 96438 MW; 217E8EAC273EEF56 CRC64;
MNLEKFTERS RGFLQAAQTI AMRESHQRLA PEHLLKALMD DEEGMASNLI RRAGGAPERV
LEAVEAALSR MPKVTGDAGQ VYMDQATGRV LDEAESLAKK AGDSFVPVER MLMALCMVPS
KAKEALDAGA VTAQNLNAAI NDIRKGRTAD TASAEDGYEA LKKYARDLTE MAEEGRIDPI
IGRDEEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE SLKDKRLMAL
DMGALIAGAK YRGEFEERLK SILNEISAAA GEVILFIDEM HTLVGAGKSE GAMDAANLIK
PALARGELHC IGATTLDEYR KHVEKDAALA RRFQPVFVEE PTVEDTVSIL RGIKEKYELH
HGVRISDAAL VAAATLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDALDRDIL
QKQIEAEALR KEDDEASKER LEKLEAELAE MQQQSTEMTA KWQAERDKLD RSRQIKEQLD
RARAELDQAK REGNLARAGE LSYGIIPQLE KALSEAESRE DDVMVAEAVR PEQIAQVVER
WTGIPTSKML EGERDKLLRM EEELGRRVIG QTEAVKAVAN AVRRARAGLN DEHRPLGSFL
FLGPTGVGKT ELTKAVAEYL FDDDQAMVRI DMSEFMEKHA VARLIGAPPG YVGYDEGGVL
TEAVRRRPYQ VILFDEVEKA HPDVFNVLLQ VLDDGVLTDG QGRRVDFKQT LIVLTSNLGS
QALSQLPDGA DAEEARREVM EAVRDHFRPE FLNRLDETVI FHRLTREDMD GIVTIQLRQL
QKRLDARGIL LDLDEGARKW LADAGYDPVY GARPLKRVIQ RSLQDPLAEA LLAGEIRDGG
NIGVTVGPEG LIIGDRVVGS NRPKPEDAVL H
//
