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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//