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Database: UniProt
Entry: A0A1G5AD81_9FIRM
LinkDB: A0A1G5AD81_9FIRM
Original site: A0A1G5AD81_9FIRM 
ID   A0A1G5AD81_9FIRM        Unreviewed;       860 AA.
AC   A0A1G5AD81;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN02910433_00090 {ECO:0000313|EMBL:SCX75797.1};
OS   Blautia sp. SF-50.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=1520805 {ECO:0000313|EMBL:SCX75797.1, ECO:0000313|Proteomes:UP000198516};
RN   [1] {ECO:0000313|Proteomes:UP000198516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF-50 {ECO:0000313|Proteomes:UP000198516};
RA   Varghese N., Submissions S.;
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; FMUW01000001; SCX75797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5AD81; -.
DR   Proteomes; UP000198516; 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:SCX75797.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SCX75797.1};
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;  96967 MW;  092A954A0A75D9F1 CRC64;
     MNISKFTQKS VQAVQDLEKI AYEYGNQEIE EEHLLYALLT QEDSLILKLI EKMEIQKEYF
     IDTVKRALDA RVKVSGGELR FGQYLNKALV SAEDEAKAMG DEYVSVEHLF LSMLKNPSPS
     MKKLFNEFGI TRERFLQALS TVRGNQRVVS DNPEATYDTL NKYGEDLVEK AKNQKLDPVI
     GRDMEIRNII RILSRKTKNN PVLIGEPGVG KTAAIEGLAQ RIVAGDVPEG LKNKKIFALD
     MGALVAGAKY RGEFEERLKA VLEEVKKSEG QIILFIDELH LIVGAGKTDG AMDAGNMLKP
     MLARGELHCI GATTLDEYRQ YIEKDAALAR RFQPVMVNEP TVEDTISILR GLKERYEVFH
     GVKITDSALV AAATLSHRYI TDRFLPDKAI DLVDEACALI KTELDSMPTE LDEQRRKIMQ
     LEIEESALKK ETDNLSKERL ADLQKELAEL RDTFNTQKAQ WDNEKHSVEK LQKLREQIED
     INKQIQKAKQ NYDLEKAAEL QYGELPKLQQ QLEIEEKQVK ESDRSLVHEA VTDDEIARII
     SRWTGIPVTK LTEGERTKLL GLEDELHKRV VGQDEGVRLV TDAILRSKAG IKDPTKPIGS
     FLFLGPTGVG KTELAKTLAA TLFDDEQNMV RIDMSEYMEK YSVSRLIGAP PGYVGYEEGG
     QLTEAVRRKP YSVVLFDEIE KAHPDVFNVL LQVLDDGRIT DSQGRTVDFK NTILIMTSNI
     GSPYLLDGID EKGDIKPEAQ EQVMNDLRGH FRPEFLNRLD EIIMFKPLTK DNVGKIVDLM
     VKELSDRLAD QELSLELTDA AKQMVVDNGY DPVYGARPLK RYLQNYVETL TAKKILSGDV
     HAGDTIVLDV KDGAFTVSTK
//
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