ID A0A0D0N7D1_KITGR Unreviewed; 867 AA.
AC A0A0D0N7D1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=TR51_29370 {ECO:0000313|EMBL:KIQ64080.1};
OS Kitasatospora griseola (Streptomyces griseolosporeus).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=2064 {ECO:0000313|EMBL:KIQ64080.1, ECO:0000313|Proteomes:UP000032066};
RN [1] {ECO:0000313|EMBL:KIQ64080.1, ECO:0000313|Proteomes:UP000032066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF730-N6 {ECO:0000313|EMBL:KIQ64080.1,
RC ECO:0000313|Proteomes:UP000032066};
RA Arens J.C., Haltli B., Kerr R.G.;
RT "Draft genome sequence of Kitasatospora griseola MF730-N6, a bafilomycin,
RT terpentecin and satosporin producer.";
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|ARBA:ARBA00004496,
CC 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:KIQ64080.1}.
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; JXZB01000004; KIQ64080.1; -; Genomic_DNA.
DR RefSeq; WP_043916596.1; NZ_JXZB01000004.1.
DR AlphaFoldDB; A0A0D0N7D1; -.
DR STRING; 2064.TR51_29370; -.
DR PATRIC; fig|2064.6.peg.6235; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000032066; 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 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:UP000032066};
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 867 AA; 94639 MW; B0BA925A2A45F406 CRC64;
MDASKFTSKT QEALSSAIRQ AGAAGNPDVK PVHILLALLE QPEGLARPLL KAVAADAAPI
AVEARRQAAA LPAAQGSTVA APQLARDTLA VLEEAGKRAA DLDDQYVSTE HLLVGLAAEG
GPVAELLKQH GATAKALLAA FKDVRGSARV TSPDPEGTYK ALEKYGSDLT QAARDGKLDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVAGDVP ESLRGKRLVS
LDLAAMVAGA KFRGEFEERL KAVLNDIKDS DGQVITFIDE LHTMVGAGAG GDSSMDAGNM
LKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVLV GEPTVEDTIA ILRGLKGRYE
AHHKVEITDA ALVAAATLSN RYITSRFLPD KAIDLVDESA SRLRMEIDSS PVEIDELQRA
VDRLRMEELA LDKESDPASV ERLGRLRRDL ADKQEQLSTL NARWEQEKKS LNRVGELKER
LDDLRGALDR AQRDGDFERA SKLMYAEIPA AERELTEAQD RAADEPNTTM VKEQVGPDDV
ADVVSSWTGI PAGRLLEGES AKLLRMEDEL GRRLIGQREA VQAVSDAVRR TRSGIADPDR
PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMVRIDMSE YGEKHSVSRL VGAPPGYVGY
EEGGQLTEAV RRRPYSVVLL DEVEKAHPEV FDVLLQVLDD GRLTDGQGRT VDFRNTILIL
TSNLGSAYLV DPATPEERKK ELVLETVRQS FKPEFLNRLD DIVVFDPLGT AELSRIVDLQ
IAALARRLHE RRLTLDVTPA ARDWLSLTGY DPAYGARPLR RLVQSAIGDQ LAKEILSGRV
HDGDTVLVDR DEANDRLSVG PKPSLVK
//
