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Database: UniProt
Entry: A0A0K8JHU4_9FIRM
LinkDB: A0A0K8JHU4_9FIRM
Original site: A0A0K8JHU4_9FIRM 
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
//
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