ID A0A1M7G4P7_9RHOB Unreviewed; 872 AA.
AC A0A1M7G4P7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05444398_1108 {ECO:0000313|EMBL:SHM11253.1};
OS Roseovarius pacificus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=337701 {ECO:0000313|EMBL:SHM11253.1, ECO:0000313|Proteomes:UP000183974};
RN [1] {ECO:0000313|EMBL:SHM11253.1, ECO:0000313|Proteomes:UP000183974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29589 {ECO:0000313|EMBL:SHM11253.1,
RC ECO:0000313|Proteomes:UP000183974};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRBR01000010; SHM11253.1; -; Genomic_DNA.
DR RefSeq; WP_073035645.1; NZ_FRBR01000010.1.
DR AlphaFoldDB; A0A1M7G4P7; -.
DR STRING; 337701.SAMN05444398_1108; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000183974; 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:SHM11253.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SHM11253.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183974};
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..529
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 95812 MW; 7D023D609A2EAA1C CRC64;
MDLNKFTERS RGFIQAAQTI AMRESHQKLA PEHLLKALMD DAEGLASNLI KRAGGDPARV
RQAVDLALGK IPQVSGDAGQ TYMDQQTGKV LAEAEKLADK AGDSFVPVER ILTALAIVKS
PAKDALEQGA ITAQKLNEAI NDLRKGRTAD SASAEDTYEA LEKYAHDLTK AAEEGKIDPI
IGRDDEIRRA MQILSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE SLRNKRLLAL
DMGALIAGAK YRGEFEERLK AILNEVTAAA GEIILFIDEM HTLVGAGKAD GAMDAANLIK
PALARGELHC IGATTLDEYR KHVEKDAALA RRFQPLVVEE PTVEDTISIL RGIKEKYELH
HGVRISDSAL VTAATLSHRY ITDRFLPDKA IDLMDEAASR LRMEVDSKPE ELDALDRDIL
QKQIEAEALR KEDDAASKDR LEKLEKELAE LQEKSSEMTA QWQAERDKLA GARDLKEQLD
KARIELDHAK REGNLARAGE LSYGVIPQLE KQLAEAEQAE DEGVMVEEAV RPEQIAQVVE
RWTGIPTAKM LEGEREKLLG MEDNLHRRVI GQDQAVKAVA NAVRRARAGL NDESRPLGSF
LFLGPTGVGK TELTKAVAEF LFDDDGAMVR IDMSEFMEKH SVARLIGAPP GYVGYDEGGV
LTEAVRRRPY QVVLFDEVEK AHPEVFNVLL QVLDDGVLTD GQGRTVDFKQ TLIILTSNLG
SQALSQMPEG ADASDAKRDV MDAVRSHFRP EFLNRLDEIV IFDRLTRDQM DGIVDIQMAR
LLKRLASRKI ALELDDGART WLADQGYDPV YGARPLKRVI QKALQDPLAE ALLAGEIRDG
DTVPVSAGAE GLLIGDRVGT SDRQPPQDAV VH
//