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Database: UniProt
Entry: A0A017HKH2_9RHOB
LinkDB: A0A017HKH2_9RHOB
Original site: A0A017HKH2_9RHOB 
ID   A0A017HKH2_9RHOB        Unreviewed;       871 AA.
AC   A0A017HKH2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=Rumeso_03447 {ECO:0000313|EMBL:EYD74982.1};
OS   Rubellimicrobium mesophilum DSM 19309.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD74982.1, ECO:0000313|Proteomes:UP000019666};
RN   [1] {ECO:0000313|EMBL:EYD74982.1, ECO:0000313|Proteomes:UP000019666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD74982.1,
RC   ECO:0000313|Proteomes:UP000019666};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (FEB-2013) 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:EYD74982.1}.
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DR   EMBL; AOSK01000096; EYD74982.1; -; Genomic_DNA.
DR   RefSeq; WP_037283899.1; NZ_KK088629.1.
DR   AlphaFoldDB; A0A017HKH2; -.
DR   STRING; 442562.Rumeso_03447; -.
DR   PATRIC; fig|442562.3.peg.3393; -.
DR   HOGENOM; CLU_005070_4_1_5; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000019666; 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 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019666};
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;  95846 MW;  D35005262B4613E4 CRC64;
     MNLEKFTERS RGFLQAAQTI AARESHQRIL PEHLLKALMD DDQGLAANLI DRSGGASARV
     REAVDAAVAR VPKVTGDAGQ AYIDTALVRV LDEAEKVATK AGDSFVPVER MLMALAMVKS
     KAQEALSAGA VTAQGLNAAI NDVRKGRTAD TASAEEGYDA LKKYARDLTE AARDGKIDPI
     IGRDEEIRRS MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE SLKNKKLLAL
     DMGALIAGAK YRGEFEERLK AILKEIEAAA GEVILFIDEM HTLVGAGKAD GAMDAANLIK
     PALARGELHC IGATTLDEYR KHVEKDAALA RRFQPILVEE PTVEDTISIL RGIKEKYELH
     HGVRISDSAL VAAATLSHRY ITDRFLPDKA IDLVDEAASR LRMEIDSKPE ELDQLDRQLL
     QLQIEAEALK KEDDAASQDR LARLEKEMAE LQERSAAMTA KWQAERDKLD RSRTIKERLE
     EARAQLDKAK REGNLAEAGR LAYGEIPQLE KELSEAEAQG DGLMVEEAVR PEQIAEVVER
     WTGIPTSRML EGEREKLLRM EEALGKRVVG QESAVAAISR AVRRARAGLN DENRPLGSFL
     FLGPTGVGKT ELTKAVAEFL FDDDTAMVRI DMSEFMEKHS VARLIGAPPG YVGYDEGGVL
     TEAVRRRPYQ VVLFDEVEKA HPDVFNVLLQ VLDDGVLTDG QGRTVDFKQT LIVLTSNLGA
     YALSQLPEGA DASAAKREVM DAVRAHFRPE FLNRLDEMII FDRLDRTDMT GIVEIQLRRL
     EQRLAQRKIA LELDAAAKQW LADEGYDPVF GARPLKRVIQ RALQDQLAEM ILAGEVKDED
     TVPVTVGPEG LIVGTRVAGT QRERPVEAVV H
//
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