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Database: UniProt
Entry: A0A1I0FPB6_9FIRM
LinkDB: A0A1I0FPB6_9FIRM
Original site: A0A1I0FPB6_9FIRM 
ID   A0A1I0FPB6_9FIRM        Unreviewed;       860 AA.
AC   A0A1I0FPB6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN04487772_1355 {ECO:0000313|EMBL:SET60194.1};
OS   [Clostridium] polysaccharolyticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=29364 {ECO:0000313|EMBL:SET60194.1, ECO:0000313|Proteomes:UP000199800};
RN   [1] {ECO:0000313|EMBL:SET60194.1, ECO:0000313|Proteomes:UP000199800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1801 {ECO:0000313|EMBL:SET60194.1,
RC   ECO:0000313|Proteomes:UP000199800};
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; FOHN01000035; SET60194.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0FPB6; -.
DR   STRING; 29364.SAMN04487772_1355; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000199800; 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:SET60194.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SET60194.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199800};
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..525
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   860 AA;  97688 MW;  B574C735F321ECCF CRC64;
     MNINKFTQKS IEAVNNCEKI AYEYGNQEIV QEHLLLSLFT IEEGLIPKLL KKMGVEMNQI
     ENEVRQLLEK RPKVSGGRVY MGEDLNKALI YAEDISKKMG DEYVSVEHLF LSIMKYANRE
     VKSLLKQFGI SQESFLQALS TVRGNQKVTS DNPENTYDTL EKYGYDLVER AKEQKLDPVI
     GRDQEIRNVI RILSRKSKNN PVLIGEPGVG KTAVVEGLAQ RIVRGDVPEN LKDKRIFALD
     MGSLVAGAKY RGEFEERLKA VLEEVKQSEG EIILFIDELH TIVGAGKTDG AMDAGNMLKP
     MLARGELHCI GATTLNEYRM YIEKDAALER RFQPVMVEEP TVEDTISILR GLKERYEVYH
     GVKITDASIV TAAALSNRYI SDRFLPDKAI DLIDEACALI KTELNSMPME IDDIQRHIMQ
     LEIEEAALKK ETDHISQERL KELQSELATL REDFALKKAK WDEEKSSVEK VQKLKEEIEE
     LHNQIQIAQR NYDLNKAAEL QYGKLPELEK QLVVEEERVK EEKRELVHES VTEEEIAKII
     ARWTGIPVAK LTESEREKTL HLDEELHKRV IGQDEGVSLV TEAILRSKAG IKDPTKPIGS
     FLFLGPTGVG KTELAKSLAA SLFDDESNMV RIDMSEYMEK YSVSRLIGAP PGYVGYEEGG
     QLTEAVRRKP YAVILFDEIE KAHPDVFNVL LQVLDDGRIT DSQGRTVDFK NTILIMTSNL
     GSSYLLEGIS EDGDIKPEAQ ESVMNELHGN FRPEFLNRLD EIIMFKPLTK QNINRIIDLL
     VADLNKRLED KELTLEVSEQ ARLCIVDNAY DPYFGARPLK RYVQKNIETL TARLILQDKV
     MPQDKIFIDV EEGKLVAKVS
//
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