ID A0A0F0HL34_9PSEU Unreviewed; 871 AA.
AC A0A0F0HL34;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=UK12_24255 {ECO:0000313|EMBL:KJK56170.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK56170.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK56170.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK56170.1,
RC ECO:0000313|Proteomes:UP000033409};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJK56170.1}.
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DR EMBL; JYJF01000089; KJK56170.1; -; Genomic_DNA.
DR RefSeq; WP_045305247.1; NZ_JYJF01000089.1.
DR AlphaFoldDB; A0A0F0HL34; -.
DR PATRIC; fig|1427391.3.peg.7457; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000033409; 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: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:UP000033409};
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 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 94585 MW; B7D3E0BE2583B30F CRC64;
MDAGKFTSKT QDALSAAIRQ ASAAGNPDVK PVHILLALLE QPEGIARPLL EAVGADVAAV
TAAARRQLGT LPSAQGSTVS APQLARDTMA VLGEAGKRAE DLDDQYLSTE HLLVGLAAEG
GPVADLLKQH GAAAKALLAA FKDVRGSARV TSPDPEGTYK ALEKYGTDLT QAARDGKLDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGDPG VGKTAVVEGL AQRIVAGDVP ESLRGKRLVA
LDLGAMVAGA KYRGEFEERL KAVLNDIKSS NGQVVTFIDE LHTMVGAGAG GDSAMDAGNM
LKPMLARGEL RMVGATTLDE YRERIEKDAA LERRFQQVLV GEPSVEDTIA ILRGLKGRYE
AHHKVQIADA ALVAAASLSN RYITARFLPD KAIDLVDEAA SRLRMEIDSS PVEIDQLQRS
VDRLRMEELA LEKESDPASV ERLDRLRRDL ADKQEQLSTL NARWEQEKKS LNRVGELKER
LDDLHGLLER AQRDGDFERA SKLMYAEIPA AEQELADAQA RAADEDAGTS MVKEEVGPDD
VADVVASWTG IPAGRLLEGE SAKLLRMEEE LGHRLIGQTE AVRAVSDAVR RTRAGLADPD
RPTGSFLFLG PTGVGKTELA KALADFLFDD ERAMVRIDMS EYGEKHSVSR LVGAPPGYVG
YEEGGQLTEA VRRRPYSVVL LDEVEKAHPE VFDVLLQVLD DGRLTDGQGR TVDFRNAILI
LTSNLGSQFL VDPSTPDERK KALVLDTVRS AFKPEFLNRL DDIVVFDALG TAELSRIVDL
QVARLGERLR ERRLTLDVTA AARDWLALTG YDPAYGARPL RRLVQSAIGD QLARAILSGE
VHDGDTVVVE RDEAGDRLTV RSQHPVTSLQ K
//