ID A0A1I7GYF4_9FIRM Unreviewed; 863 AA.
AC A0A1I7GYF4;
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=SAMN05216508_11017 {ECO:0000313|EMBL:SFU53420.1};
OS Eubacterium pyruvativorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=155865 {ECO:0000313|EMBL:SFU53420.1, ECO:0000313|Proteomes:UP000198817};
RN [1] {ECO:0000313|EMBL:SFU53420.1, ECO:0000313|Proteomes:UP000198817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHGC13 {ECO:0000313|EMBL:SFU53420.1,
RC ECO:0000313|Proteomes:UP000198817};
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; FPBT01000010; SFU53420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7GYF4; -.
DR STRING; 155865.SAMN05216515_11135; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198817; 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:SFU53420.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFU53420.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198817};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 97394 MW; 3D4D6D09384C3553 CRC64;
MNFEKYTQNA RQAVVDAQSL AVQYGQQEID GEHLHLALMQ QRDGLIPKLV KNMGADPGQI
IRELEDALGR LPKVSGSAQN AYFSRRAEKL LNDAEKETKN FRDDYTTVDH LYLALLREKR
TPSAEIFGRH GITKQKFLEE LMKVRGNQRV TSDNPEDNYD ALEKYGRDLV DLAKENKLDP
VIGRDEEIRH LIQILSRKTK NNPVLIGEPG VGKTAVVEGL AQRILREDVP ENLKDKTIFE
LDMGALIAGA KFRGEFEERL KTVLNEIEKS DGKIILFIDE IHNIVGAGRT EGSMDAGNLL
KPKLARGELH CIGATTLDEY RKYMEKDKAL ERRFQKVMVG EPSVEDTISI LRGLRDTFER
HHKVNITDSA LIACATLSDR YISDRFLPDK AIDLMDEAAA RIRTQIDSKP MELDEISRKI
TQMEIERQSL SKETDKGSKT RLDALEKELA QLKDRQKAMN AQWEGEKQEI EDTKELREKL
DQARFDLEQA KRSYDYNRAA ELQNGTIPEL EKKIEASKEA AEHGRDSSLL NVEVGENEIA
EVVSQWTGIP VAKLVETERE KLLNLPEILH HRVVGQDEGV DAVSDAILRA RAGLKDENRP
IGSFIFLGPT GVGKTELAKT LSEALFDSEK NLIRIDMSEY MEKHSVSRLV GAPPGYVGYD
EGGQLTEAVR RHPYSVILFD EIEKAHPDVF NILLQLLDDG RLTDNQGRTV DFKNTVVIMT
SNIGSSDLID NIREDGKIDD AVKERVVKSL RSYFKPEFLN RVDDIVVFSP LTIEQVKKII
DLDMDALEKR LAQRDMKLTI TDSAKQYIAE QSYDPNYGAR PVKRYLQTAV ENQLARMIIS
GEISDGSGIS VDAGAEGLTF HCV
//