ID A0A1B4VAM7_9GAMM Unreviewed; 869 AA.
AC A0A1B4VAM7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SVA_2224 {ECO:0000313|EMBL:BAU48774.1};
OS Sulfurifustis variabilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Acidiferrobacterales;
OC Acidiferrobacteraceae; Sulfurifustis.
OX NCBI_TaxID=1675686 {ECO:0000313|EMBL:BAU48774.1, ECO:0000313|Proteomes:UP000218899};
RN [1] {ECO:0000313|EMBL:BAU48774.1, ECO:0000313|Proteomes:UP000218899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=skN76 {ECO:0000313|Proteomes:UP000218899};
RA Miura A., Kojima H., Fukui M.;
RT "Complete genome sequence of Sulfurifustis variabilis.";
RL Submitted (AUG-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}.
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DR EMBL; AP014936; BAU48774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B4VAM7; -.
DR KEGG; sva:SVA_2224; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000218899; Chromosome.
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:UP000218899};
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..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 869 AA; 96632 MW; EF9D2040724288BE CRC64;
MRMDKLTAKF QTALAEAQSL ALGRDHQFIE PVHLMAALLD QEGGTTRQLL AQADVNVNAV
RSKVAEALDR LGTVHGAGGE VHVSNDLGKL LNLTDKYAQK RGDQYISTEL FLLAALEDQG
ELGRILREAG ASRNGIEKAL EAMRGGQKVD DPNAEDTRQA LSKYTVDLTE RAEQGKLDPV
IGRDEEIRRV VQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKNKRVLAL
DMGALIAGTK FRGEFEERLK AVLNELARQQ GQIILFIDEL HTIVGAGKAE GAMDAGNMLK
PALARGELHA VGATTLDEYR KHIEKDAALE RRFQKVLVDE PTVEDTIAIL RGLKEKYEVH
HGVDITDPAI VAAATLSHRY ITDRQLPDKA IDLVDEAASR IRMEIDSKPE AMDRLDRRLV
QLKIEREALK KETDEASKKR LALLEDEIER LEQEYGELEG IWKAEKAQVT GAAHVKEELD
RARLELDTAR RAGDLGRMAE LQYGRIPELE KQLAAASSQE SQKTEKKLLR NAVTENEIAE
VVSRWTGIPV SKMMEGERDK LLRMEDDLRR RVVGQDEAIK AVSNAIRRSR AGLSDPRRPY
GSFLFLGPTG VGKTELTKAL AAFLFDTDEA MVRLDMSEFM EKHSVARLIG APPGYVGYEE
GGYLTEAVRR KPYSVILLDE VEKAHPDVFN VLLQVLDDGR LTDGQGRTVD FRNTVIIMTS
NLGSTVIQEL AGEENYQKMK DAVMQIVGQH FRPEFINRVD DIVVFHPLGR DQLHRIAELQ
VQYLRGRLKS REMDLELTKA ALDKLAEAGY DPVYGARPLK RAIQQAIENP LAQEILAGKF
GPKDVILVDV AGDRLAFRKK LAGAEKKTA
//
