ID B9KY98_THERP Unreviewed; 870 AA.
AC B9KY98;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=trd_0443 {ECO:0000313|EMBL:ACM06295.1};
OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC Bacteria; Thermomicrobiota; Thermomicrobia; Thermomicrobiales;
OC Thermomicrobiaceae; Thermomicrobium.
OX NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM06295.1, ECO:0000313|Proteomes:UP000000447};
RN [1] {ECO:0000313|EMBL:ACM06295.1, ECO:0000313|Proteomes:UP000000447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27502 / DSM 5159 / P-2
RC {ECO:0000313|Proteomes:UP000000447};
RX PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA Eisen J.A.;
RT "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT Thermomicrobium roseum.";
RL PLoS ONE 4:E4207-E4207(2009).
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; CP001275; ACM06295.1; -; Genomic_DNA.
DR RefSeq; WP_012641848.1; NC_011959.1.
DR AlphaFoldDB; B9KY98; -.
DR STRING; 309801.trd_0443; -.
DR KEGG; tro:trd_0443; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000000447; 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:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; IPR017729; ATPase_T6SS_ClpV1.
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 InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR001806; Small_GTPase.
DR NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR NCBIfam; TIGR03345; VI_ClpV1; 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.
DR PROSITE; PS51421; RAS; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 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 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 574..829
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT COILED 413..534
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 870 AA; 99144 MW; 6E183C773EC8FEEF CRC64;
MGRPQFTEKA QEALVTAQRT AAERQNSQLD VEHLLYALVT QHDGVVPQVL LRLQLDPRRV
AQELERVLET LPRLQYAAEP TISPVLRRVL ERAQSEAQSF GDQYISTEHL LLAALDAAPR
SPAVQALARL GVQRERVLEA LSQIRGAQRV TSPNPESTYQ ALERYGRDLT ALARQGKLDP
VIGRDDEIRR VIQVLLRRTK NNPVLIGEPG VGKTAIVEGL AQRIVRGDVP EGLRDKRIVQ
LDLAAMLAGA KYRGEFEERL KAVLDEIRAS EGEIIVFIDE VHTVVGAGAA EGAMDAANML
KPMLARGELH AIGATTLDEY RKHIEKDPAL ERRFQPVFVD EPSVEDTISI LRGLRERYEL
HHKVRILDSA LVAAAVLSHR YITNRFLPDK AIDLVDEAAA RLRMEITSMP AELDELTRRI
TQLEIEREAL RKERDEASRQ RLAELERELA NLREQEQVLR SQWEQERQAL ERINALKEQI
EQTRIEIEQA LRAADYTRAS ELQYGRLVEL ERQLREEERR LADVQRQGRL LKEEVDADDI
AEIVSKWTGI PVAKLMEGEM EKLVHMEERL HERVVGQDEA VRAVSNAIRR ARAGLQDPNR
PLGSFIFLGP TGVGKTELAR ALAEFLFDDE RAMVRIDMSE YQERHTVSRL IGAPPGYVGY
EEGGQLTEAV RRRPYSVVLF DEIEKAHPEV FNVLLQVLDD GRLTDGQGRT VDFRNTVIIM
TSNLGSEYIQ ALLPHREEEA YERVMQAVRA HFRPEFLNRI DEIIMFRPLT REQLSQIVDI
QLRQVRQRLK QRNITLQVTL RAKEWLAERG YDPVYGARPL KRVIQRELLD PLANMLLRGE
VRDGETVLVD VDEHGNLSIR SMLAEAEVVA
//
