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Database: UniProt
Entry: D4JRU3_9FIRM
LinkDB: D4JRU3_9FIRM
Original site: D4JRU3_9FIRM 
ID   D4JRU3_9FIRM            Unreviewed;       867 AA.
AC   D4JRU3;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=EUS_05170 {ECO:0000313|EMBL:CBK95812.1};
OS   [Eubacterium] siraeum 70/3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Oscillospiraceae incertae sedis.
OX   NCBI_TaxID=657319 {ECO:0000313|EMBL:CBK95812.1, ECO:0000313|Proteomes:UP000008803};
RN   [1] {ECO:0000313|EMBL:CBK95812.1, ECO:0000313|Proteomes:UP000008803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70/3 {ECO:0000313|EMBL:CBK95812.1,
RC   ECO:0000313|Proteomes:UP000008803};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Eubacterium siraeum 70/3.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK95812.1, ECO:0000313|Proteomes:UP000008803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70/3 {ECO:0000313|EMBL:CBK95812.1,
RC   ECO:0000313|Proteomes:UP000008803};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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. {ECO:0000256|RuleBase:RU362034}.
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; FP929044; CBK95812.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4JRU3; -.
DR   KEGG; esu:EUS_05170; -.
DR   PATRIC; fig|657319.3.peg.739; -.
DR   HOGENOM; CLU_005070_4_0_9; -.
DR   Proteomes; UP000008803; 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          4..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          417..531
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   867 AA;  97177 MW;  3078238B977B4E5A CRC64;
     MLNTNNLTQK SMEAISTAQS IAVSYQNMNI EQQHILLALL QAEDGLIPQL IKKMGADASQ
     LTRLTEQSAA GIPKVTGSGR DPEKVYVSPD VDKAFTAAEE KAKQMKDEYI SVEHLFIGLL
     EKPNSQLKDI FAKCGITEKA FLQALEQVRG SVRVTGQNPE ETYDVLKKYG QDLTELARQN
     KLDPVIGRDT EIRNVIRILS RKTKNNPVLI GEPGVGKTAI AEGLALRIVR GDVPENLKER
     QIFSLDMGAL VAGAKYRGEF EERLKAVLQT IKKSEGQIIL FIDELHTIVG AGKTDGAMDA
     GNLLKPLLAR GELHCIGATT LNEYRQYIEK DAALERRFQP VMVNEPTVED TISILRGLKE
     RYEVFHGVKI HDSALIAAAT LSDRYISDRF LPDKAIDLVD EACALIKTEM ESMPSELDDI
     RRKIMQHEIE EAALKKETDR ISVEHLAEVQ QELAEMRSKF NEMKAKWENE RNAISKVQKL
     REEIESTNSL IEQAERSYDL NKAAELKYGK LPQLQKELEE EEKLAEQSKS ASMLHDKVTE
     EEIAKIICRW TGIPVSKLME GEREKLLHME DILHKRVIGQ DEAVEKVSEA ILRSRAGIAN
     PDQPIGSFLF LGPTGVGKTE LAKALAEALF DDEHSMVRID MSEYMEKFSV SRLIGAPPGY
     VGYEEGGQLT EAVRRKPYSV VLLDEVEKAH PDVFNILLQI LDDGRITDSQ GRTVDFKNTI
     IILTSNLGSS YILDGINEKG EISEEAKNEV NKLLKTQFRP EFLNRLDEIV FYKPLRKDEI
     SGIVDLMLGE LKKRLADKEV GFAITDAAKD YVIDNGFDPN YGARPLKRFI QRKIETLIAR
     KLIADDVAPG STLTVDYDGE KLICSES
//
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