ID A0A1H1EGQ9_9ACTN Unreviewed; 872 AA.
AC A0A1H1EGQ9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05428996_3004 {ECO:0000313|EMBL:SDQ87991.1};
OS Quadrisphaera sp. DSM 44207.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Quadrisphaera.
OX NCBI_TaxID=1881057 {ECO:0000313|EMBL:SDQ87991.1, ECO:0000313|Proteomes:UP000199015};
RN [1] {ECO:0000313|EMBL:SDQ87991.1, ECO:0000313|Proteomes:UP000199015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44207 {ECO:0000313|EMBL:SDQ87991.1,
RC ECO:0000313|Proteomes:UP000199015};
RA de Groot N.N.;
RL Submitted (OCT-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; FNKA01000004; SDQ87991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1EGQ9; -.
DR STRING; 1881057.SAMN05428996_3004; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199015; 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:SDQ87991.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDQ87991.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199015};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..519
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 94320 MW; 6ABA35C6F3149975 CRC64;
MELKLTTKSQ EAMAAAASRA VQAGHPQVEP AHLLAALLQQ GGVATALLQA VGADPAALRP
RADALLAALP SASGSSVAAP QLSRPALTAL TTARTESEAM GDAFVSADHL VLGLAADQGA
TGEALRAAGA TPEALREALP TVRGGAKVTS ADPEGTFNAL EQYGVDLTAR AREGAIDPVI
GRDAEIRRVV QVLSRRTKNN PVLIGEPGVG KTAVVEGLAQ RIVDGDVPES LRGKRLVSLD
LGAMVAGAKY RGEFEERLKA VLEEIRGSQG QVITFIDELH TVVGAGAGGD SSLDAGNMLK
PMLARGELRL VGATTLDEYR ERIEKDPALE RRFQQVFVGE PSVEDTVAIL RGLNERYEAH
HKVEITDAAL VAAATLSSRY ISGRQLPDKA IDLVDEAASR LRMEIDSSPV EIDELRRSVD
RLRMEELALE QEEDEASRER LQRLRADLAD RTERLAGLMA RWEQQKAGLN RVGELKAALD
DARVRYERAV RDTDYETASR IQYGEIADLE RQLEQAQAAE AQASPSDDRM VAERVGPDDI
AEVVSAWTGI PVGRLMEGET GKLLRMEEVL GERLVGQAEA VRAVSDAVRR SRAGVSDPDR
PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMIRIDMSE YGEKHSVARL VGAPPGYVGY
EAGGQLTEAV RRRPYSVVLL DEVEKAHPEV FDVLLQVLDD GRLTDGQGRT VDFRNTILIL
TSNLGSQFLV DLTLDKESQR AAVMDVVRRT FKPEFLNRLD EVVVFDALGT GELGRIVDLQ
VARMAGRLAE RRLRLQVTDA AREWLALEGW DPAYGARPLR RLVQREIGDQ LAWALLSGEV
RDGDTVLVDR TAEDGGASGL LVRRAEEPAP AA
//
