ID A0A1M6VL19_PSETH Unreviewed; 869 AA.
AC A0A1M6VL19;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05443637_112194 {ECO:0000313|EMBL:SHK82159.1};
OS Pseudonocardia thermophila.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1848 {ECO:0000313|EMBL:SHK82159.1, ECO:0000313|Proteomes:UP000184363};
RN [1] {ECO:0000313|EMBL:SHK82159.1, ECO:0000313|Proteomes:UP000184363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43832 {ECO:0000313|EMBL:SHK82159.1,
RC ECO:0000313|Proteomes:UP000184363};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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|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; FRAP01000012; SHK82159.1; -; Genomic_DNA.
DR RefSeq; WP_073458058.1; NZ_FRAP01000012.1.
DR AlphaFoldDB; A0A1M6VL19; -.
DR STRING; 1848.SAMN05443637_112194; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000184363; Unassembled WGS sequence.
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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:SHK82159.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SHK82159.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184363};
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 869 AA; 94305 MW; 5172F58E75A21EC6 CRC64;
MDSFNPTTKT QQAISSAVQA ASLAGNPEVG PTHLLGALLA QADGIAVPLL EAVGADVAAV
RAGLTQLGNR LPSASGSTVG PPQMSRAALN AINAAQQLAT EMGDEYVSTE HLLVGLAKAG
GPVADLLARH GATPEALREG FTKVRGSSRV TSPDPEGTYQ ALQKYGVDLT ERARNGELDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVAGDVP ESLRGKKVVA
LDLGSMVAGA KYRGEFEERL KAVLKEITES AGQIITFIDE LHTIVGAGAT GEGAMDAGNM
IKPMLARGEL RLVGATTLDE YRQHIEKDPA LERRFQQVYV GEPSVEDTIG ILRGLKERYE
VHHGVRITDA ALVAAATLSD RYITARYLPD KAIDLVDEAA SRLRMEIDSR PVEIDTVERA
VRRLEIEEMA LEKESDPASA DRLKALRQEL AEKREELSAL TARWQREKAA IEETRALAAK
LEQLRGEYER ADRDGDLEKA SELLYGRIPE VEKKLAAATA STKSEDVMLK EEVGPDDVAD
VVSAWTGVPA GRMLEGETAK LLRMEEELGK RVVGQIEAVR AVSDAVRRAR SGIADENRPT
GSFLFLGPTG VGKTELAKAL AEFLFDDERA MVRIDMSEYS EKHSVARLVG APPGYVGYDQ
GGQLTEAVRR RPYSVVLFDE VEKAHPDVFD TLLQVLDDGR LTDGQGRTVD FRNTILVLTS
NLGSQAIADP SLDDKERKDA VMAIVRQHFK PEFLNRLDDV VVFHALSTEE LTHIVDIQLR
RLRDRLAKKR LTLDVSDAAR EWLALNGFDP VYGARPLRRL VQSAIGDQLA KQLLSGDVRE
GDTVRVDLDP SAEGGTGGLI VGRALPVTV
//
