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Database: UniProt
Entry: A0A1G8PLK4_9FIRM
LinkDB: A0A1G8PLK4_9FIRM
Original site: A0A1G8PLK4_9FIRM 
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}.
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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
//
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