ID A0A1G8PLK4_9FIRM Unreviewed; 858 AA.
AC A0A1G8PLK4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN04487760_101255 {ECO:0000313|EMBL:SDI93262.1};
OS Lachnospiraceae bacterium G41.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1200749 {ECO:0000313|EMBL:SDI93262.1, ECO:0000313|Proteomes:UP000199016};
RN [1] {ECO:0000313|EMBL:SDI93262.1, ECO:0000313|Proteomes:UP000199016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G41 {ECO:0000313|EMBL:SDI93262.1,
RC ECO:0000313|Proteomes:UP000199016};
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|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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; FNEU01000001; SDI93262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8PLK4; -.
DR STRING; 1200749.SAMN04487760_101255; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199016; 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 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 Hydrolase {ECO:0000313|EMBL:SDI93262.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDI93262.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199016};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 411..491
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 858 AA; 95914 MW; 144571CC28B2AA7C CRC64;
MNITKFTQNS QNSVNMAQQY AIEFGNQEIE EEHLLYALIN IDDSLILKLI EKMEINTEHF
KARVKEAVEK RVKVSGGDLR IGQKLNEVLI TAENQAKKMG DEYVSVEHLF LSMLDHPNKE
IGEIFREYGI TKERFLTALS SVRGNVKVTS DNPEGTYDAL NKYGQDLVQK AKSRKMDPII
GRDSEIRNVI RILSRKTKNN PVLIGEPGVG KTAVAEGLAQ RIVNGDVPDD LKNKTIFALD
MGSLIAGAKY RGEFEERLKA VLDEVKSSNG EIILFIDELH TIVGAGKTDG ALDAGNMLKP
MLARGELHCI GATTLDEYRM YIEKDAALER RFQPVMVNEP TVEDTISILR GIKDRYEVYH
GVKIMDNALV AAAVLSDRYI SDRFLPDKAI DLVDEACAMI KTELNSLPTE LDEKQRKILQ
MEIEAQALKK EDDSQSEQRL ADLLADLAVE KEDFANAKAK WENEKSAVDK LSKMREEIDA
LNSKIEIAKR EGDLAKAAEL TYGELPRLKA SLEEAEKLAE KKDDSLVHEK VTDTEIARIV
SRWTGIPVAK LNESERNKVL HLADELHKRV IGQDDGVTKV TESIIRSKAG IKDPTKPIGS
FLFLGPTGVG KTELAKALAQ SLFDDENNIV RIDMSEYMEQ YSVSRLIGAP PGYVGYDEGG
QLTEAVRRKP YSVVLFDEVE KAHPDVFNVL LQVLDDGRIT DSHGKTVDFK NTIIIMTSNI
GADVLLEGID ENGEFKEGVE EAVTGMLHKF FRPEFLNRID ETILFKPLGR NEIAGILDLI
VADLNKRLED REYKVMLTDE AKDKVIAEGY NPNYGARPLK RYVQKTVETL AAKLILSGNV
SEGDTITIDV EDGKFTAR
//