ID A0A2I0N3R3_9CLOT Unreviewed; 867 AA.
AC A0A2I0N3R3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ABB02_00034 {ECO:0000313|EMBL:PKK40701.1};
OS Clostridiaceae bacterium JG1575.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae.
OX NCBI_TaxID=1658742 {ECO:0000313|EMBL:PKK40701.1, ECO:0000313|Proteomes:UP000237298};
RN [1] {ECO:0000313|EMBL:PKK40701.1, ECO:0000313|Proteomes:UP000237298}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG1575 {ECO:0000313|EMBL:PKK40701.1,
RC ECO:0000313|Proteomes:UP000237298};
RA Nelson M.C., Graf J.;
RT "Draft genome of Clostridiaceae bacterium JG1575.";
RL Submitted (OCT-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:PKK40701.1}.
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DR EMBL; LQGW01000001; PKK40701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0N3R3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000237298; 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:UP000237298};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 97010 MW; 399DB0F8759B5F86 CRC64;
MDYEKMTKNS VGAVNDALNI CVSRGNAQIE DIHLLYGLVK DEDGLICNIL RKSGLSSKAF
REDVLSAIDR KPKVSGSTQT GLSQATNRVL MEAEDIAQKM GDQYVSVEHL LLALFGTASP
EVRALFTKYS LRKDAFMMHL KEIRGSQRVT SDSPEATYEA LARFSTDLTE LARENKLDPV
IGRDEEIRHA IRILSRKTKN NPVLIGEPGV GKTAVVEGMA QRIVKGDVPE NLKNVKICSL
NMGSLLAGSK YRGEFEERLK AILDEVKAAQ GGIILFVDEI HNIVGAGKTE GSMDAGNMLK
PMLARGELRC IGATTLDEYR EYIEKDSALE RRFQPVLVDE PTVEETIAIL RGLKERYEIY
HGVTIMDSAL IEAAVLSDRY ISDRFLPDKA IDLVDEACAL IKTELNSMPT ELDSIRREIM
VLEIEAASVT KETDEASRHR LEELQKDIAG RKDEFHRLKA KWEEEKSAIG QVNELKEQIE
TLNFEISEAE RQYDLNRAAE LKYGKLPEAL KKLEAVQEEA QTKEAATLLR EKVTPEEIAK
IVSRWTGIPV SRMLEGERQK LLQLEDVLHR RVIGQDEAVT KVTEAILRSR AGIKDPNRPI
GSFLFLGPTG VGKTELAKTL AEVLFDSEQN MVRIDMSEYM EKHTVARLIG APPGYIGYEE
GGQLTEAVRR KPYSVILFDE IEKAHRDVFN ILLQVLDDGR ITDSQGRTVD FKNTVIILTS
NIGSQYLIEG MDREGHLSDA AVQNVMLELR AAFRPEFLNR LDEIVMYKPL TREEIKKILD
LMLQGIGRRL ADKNITLVLD DAAKDFVVQE GYNPIYGARP LRRYLQSSVE TLLARGIIQG
DIDQGQTVTF TVQNGALAIK ANPPEAS
//