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Database: UniProt
Entry: D5XDE6_THEPJ
LinkDB: D5XDE6_THEPJ
Original site: D5XDE6_THEPJ 
ID   D5XDE6_THEPJ            Unreviewed;       868 AA.
AC   D5XDE6;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=TherJR_0928 {ECO:0000313|EMBL:ADG81794.1};
OS   Thermincola potens (strain JR).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Thermincolaceae;
OC   Thermincola.
OX   NCBI_TaxID=635013 {ECO:0000313|EMBL:ADG81794.1, ECO:0000313|Proteomes:UP000002377};
RN   [1] {ECO:0000313|EMBL:ADG81794.1, ECO:0000313|Proteomes:UP000002377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JR {ECO:0000313|EMBL:ADG81794.1,
RC   ECO:0000313|Proteomes:UP000002377};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.;
RT   "Complete sequence of Thermincola sp. JR.";
RL   Submitted (MAY-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; CP002028; ADG81794.1; -; Genomic_DNA.
DR   RefSeq; WP_013119813.1; NC_014152.1.
DR   AlphaFoldDB; D5XDE6; -.
DR   STRING; 635013.TherJR_0928; -.
DR   KEGG; tjr:TherJR_0928; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_9; -.
DR   OMA; GPEHILM; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000002377; 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 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:UP000002377};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..527
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   868 AA;  97384 MW;  9F37C518565063C5 CRC64;
     MDLHRYTQKS REALAGAQQL AAQRHHQEVT GKHLLAVLLT QEGGMAPRFL EHAGVNVGAL
     AAGVEGLLKK IPVVTGYEGS LYAGSGFTRT LARAEQEARD MKDDYVSVEH LLLALLEDGE
     PELKEVLRRN GLTRENLLHS LRSIRGNQRV TGENPEETYE ALEKYGRDLT KLARQGKLDP
     VIGRDEEIRR VIEILSRRTK NNPVLIGEPG VGKTAIVEGL ARRIVAGDVP EGLKDKVLIG
     LDMGALIAGA KYRGEFEERL KAVLKEVQES NGKIILFIDE LHTVVGAGAA EGAVDAGNLL
     KPMLARGELR TIGATTLDEY RKHVEKDAAL ERRFQPVLVN PPSVEDTISI LRGLKERYEV
     HHGVRIKDSA IVAAAVLSDR YISDRFLPDK AIDLMDEAAA RIRTEIDSLP TELDEITRRI
     MQMEIEEAAL SKEKDEASQE RLEKLRSQLA ELRSEADAMK AQWEVEKQAI SRLREIKKEI
     EETRQEIERA EREYDLNRLA ELRYGKLANL ERQLKEEEET LAGKQKHGML LKEEVDEEDI
     ARVVSRWTGI PVSRLMAGEK EKLIHLDEEL HKRVVGQDEA VRAVADAVLR ARAGIKDPNR
     PIGSFIFLGP TGVGKTELAR ALAQALFDDE RNMIRLDMSE YMEKHTVARL IGAPPGYVGY
     EEGGQLTEAV RRKPYSVVLL DEIEKAHNDV FNVLLQLLDD GRLTDGQGRT VNFQNTVVIM
     TSNLGSQEIL AQRERGGDYE QMKESVLGIL RQYFRPEFLN RVDEIVVFHA LKQEQVKEIA
     RLLMEKLAAR VYAGAGVKLE WTENALTYLA DKGYEPSYGA RPLKRLIQQE VETPLSRMLV
     KGEISDKETV VLQAENGVLT FTKKTESK
//
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