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Database: UniProt
Entry: A0A2I0N3R3_9CLOT
LinkDB: A0A2I0N3R3_9CLOT
Original site: A0A2I0N3R3_9CLOT 
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
//
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