ID F4CV89_PSEUX Unreviewed; 871 AA.
AC F4CV89;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Psed_6547 {ECO:0000313|EMBL:AEA28635.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA28635.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA28635.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
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|ARBA:ARBA00004496,
CC 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; CP002593; AEA28635.1; -; Genomic_DNA.
DR RefSeq; WP_013678517.1; NC_015312.1.
DR AlphaFoldDB; F4CV89; -.
DR STRING; 675635.Psed_6547; -.
DR KEGG; pdx:Psed_6547; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_11; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000007809; 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 Reference proteome {ECO:0000313|Proteomes:UP000007809};
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 COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 93993 MW; C6AAB82C0BD30A7F CRC64;
MDAFNPTTKT QQAISAAAQA ATLAGNPDVG PTHLLGALLA QGDGIAAPLL EAVGADAAAV
RAELTQLGQR LPAAAGSTVS APQLSREALA AITAAQQLAT EMGDEYVSTE HLLVGLADKG
GPVADLLRRH GATPDALREA FTKVRGSSRV TSPDPEGTYQ ALEKYGQDLT ARAREGKLDP
VIGRDTEIRR VVQVLSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVAGDVP ESLRDKRVVA
LDLGSMVAGA KYRGEFEERL KAVLKEITDS AGEIITFIDE LHTIVGAGAT GEGAMDAGNM
IKPMLARGEL RMVGATTLDE YRQHIEKDPA LERRFQQVLV GEPSVEDTVG ILRGLKERYE
VHHGVRITDA ALVAAATLSD RYITARFLPD KAIDLVDEAA SRLRMEIDSR PVEIDTVERA
VRRLEIEEMA LEKESDAASK ERLAALRSEL AEKREQLSAL TARWQNEKGA IEATRELAAQ
LEQLRGEYER ADRDGDLGRA SELLYGRIPA LEKELAAKTA DVERTEDVML KEEVGPDDVA
DVVSAWTGIP AGRMLEGETA KLLRMEDELG KRVVGQAEAV RSVSDAVRRA RAGIADENRP
TGSFLFLGPT GVGKTELAKA LAEFLFDDER AMVRIDMSEY SEKHSVARLV GAPPGYVGYD
QGGQLTEAVR RRPYTVVLFD EVEKAHPDVF DTLLQVLDDG RLTDGQGRTV DFRNTILVLT
SNLGSQAIAD PALDDAARKD AVMSVVQRHF KPEFLNRLDD VVVFHALSTE ELTHIVDIQL
GVLGNRLARR RLTLDVSDAA REWLAMNGFD PVYGARPLRR LVQSSIGDQL AKELLAGAVR
EGDTVRVDLD PSAAGGTGGL IVGRASSPVT V
//
