ID A0A0K8JHU4_9FIRM Unreviewed; 859 AA.
AC A0A0K8JHU4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:CUH97085.1};
GN ORFNames=P22_3211 {ECO:0000313|EMBL:CUH97085.1};
OS Propionispora sp. 2/2-37.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Propionispora.
OX NCBI_TaxID=1677858 {ECO:0000313|EMBL:CUH97085.1, ECO:0000313|Proteomes:UP000041641};
RN [1] {ECO:0000313|EMBL:CUH97085.1, ECO:0000313|Proteomes:UP000041641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2/2 {ECO:0000313|EMBL:CUH97085.1};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) 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; CYSP01000015; CUH97085.1; -; Genomic_DNA.
DR RefSeq; WP_054261203.1; NZ_CYSP01000015.1.
DR AlphaFoldDB; A0A0K8JHU4; -.
DR STRING; 1677858.P22_3211; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000041641; 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:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000041641};
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..534
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 859 AA; 96206 MW; AFE92CADE0E2B7F3 CRC64;
MAQEKYTQEA MAVLSAAQQN CALYYHQEVT TRHLLLALIK DEEGITSRLL RDAGVDRKAI
KKEVEKLLKS IPAVRGQESG LRMNTAMIRV MALAENMAEN LQDEEIGSEH LLLAVVDDGD
SDVVDLCRRF GLHRSRLQQM LSTYRQGQDI SSGNTDQAFR ALAKYGRDLT ALAREGKLDP
VIGRDEEIRR VVEILSRRTK NNPVLIGEPG VGKTAIVEGL ARRMVAGDVP ESLKDKVLYS
LDLSSLLAGA KFRGEFEERL KNVLDEIRKA DGRVILFIDE LHTVVGAGAA EGAMDAGNIL
KPMLARGELR CIGATTLNEY RAHIEKDPAL ERRFQPVTVG EPTVEDTISI LRGLKERYEV
HHGVKIKDAA LIAAAVLSDR YISDRFLPDK AIDLVDEAAA KLRTEIDSMP SELDEVSRRI
LQLEIEEQAL RKETDAAARG RLAGIETELR ELRSHADSLR GQWDIEKQAI VRLRELKKQL
EAVRIDMENA ERAYDLNRLA ELKYGRLPAL EKELRREEEA LAKKRKQKVL LKEEVDEDDV
AKIVNRWTGI PVSRMLSGER EKLANLETIL HERVVGQEQA VKAVSEAIIR ARAGIKDPNR
PIGSFIFLGP TGVGKTELAK TLAEVLFDDE RSMIRIDMSE YMEKHAVARL IGAPPGYVGY
DEGGQLTEAV RRRPYSVLLL DEIEKAHPDV FNILLQILDD GRLTDSKGRT VDFKNTVIIM
TSNLGSAEIL NKEGEAAQEA VFAILKGYFR PEFLNRIDDI IVFKALTERQ VRKIAGMLLR
NLEKRLQKQL NLTLVWDEAV ENLLARDGYD PAFGARPLKR LISRTVETEL GRKIVSGEVA
EEGTVRLAAS HGQIIVRGK
//