ID A0A5B8XD28_9RICK Unreviewed; 864 AA.
AC A0A5B8XD28;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=Deia_00431 {ECO:0000313|EMBL:QED23232.1};
OS Candidatus Deianiraea vastatrix.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Candidatus Deianiraeaceae; Deianiraea.
OX NCBI_TaxID=2163644 {ECO:0000313|EMBL:QED23232.1, ECO:0000313|Proteomes:UP000321934};
RN [1] {ECO:0000313|EMBL:QED23232.1, ECO:0000313|Proteomes:UP000321934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CyL4-1 {ECO:0000313|EMBL:QED23232.1};
RX PubMed=31073215; DOI=.1038/s41396-019-0433-9;
RA Castelli M., Sabaneyeva E., Lanzoni O., Lebedeva N., Floriano A.M.,
RA Gaiarsa S., Benken K., Modeo L., Bandi C., Potekhin A., Sassera D.,
RA Petroni G.;
RT "Deianiraea, an extracellular bacterium associated with the ciliate
RT Paramecium, suggests an alternative scenario for the evolution of
RT Rickettsiales.";
RL ISME J. 13:2280-2294(2019).
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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
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; CP029077; QED23232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B8XD28; -.
DR Proteomes; UP000321934; Chromosome.
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 78, MITOCHONDRIAL; 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:UP000321934};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 5..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 415..495
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 864 AA; 96683 MW; 13F3DED1253CB0EF CRC64;
MSINFEKYTN SARDLVNEAV KIATSMQHSS TGPEHILQAM LTNRESIVPN LLFSAKCSVS
LLREKLQEIL DNNSVLSNGG STPYLSREAV ICLTKAEQIA KQRSDEYTTV ESILHGMLAS
KELKISKILQ ESGLVEPSLK AAIDEMRKGG SANSQDAENQ YNALKKYTRN LTELAKNGKI
DPVIGRDEEI RRTIQVLSRR IKNNPLLIGE PGVGKTAIIE GLAMRISKGD VPENLKNKTL
LELDMALVVA GAKYKGEFEE RFKAIINEVE KADGDIVLFI DEIHILMGAG GGGGAMDASN
MLKPALARGQ MHCIGATTLN EYKKYIEKDP AFARRLQTVF VSQPNVEDAI TILRGIKEKY
EMHHGVRITD SAIIAAVMMS NKYITDRFLP DKAIDLMDEA ASRLKMQIDS KPEKIDNLDR
KILQLKIEIE ALKKEDDNAS KKRMDAANIE LDTLQRELVE FTSIWQSEKL KLNKIKELKM
KLEDAKFELE KCQQSGNLAR AGELRYSVIP HLENEIKTNQ GEDGTSFIRE TITSDDIAAV
ISKATGIPLE KMLTSEKEKL LHLEDDLKAR VVGQDQAVEI IANAIRRSRS GLSSDNKPIG
SFLFLGPTGV GKTELTKAVA NMLFNDDKAM LRLDMSEYME KHSVSRLIGA PPGYVGYDEG
GVLTESIRRR PYQVVLFDEV EKAHPDVFNI LLQLLDDGRL TDSQGRTADF TNTIVILTSN
LGAQFINSND AVNNFDKMKE SVMSEVQRFF RPEFLNRLDE IIFFNRLKKE NIAGILDIQI
REIEEKLRRQ ELSIIFQQKA KDLLCDMGYD EIFGARPLKR VLQKQIYDSL ANIILQGNFK
PGDKIGVGTK DGSIILGKVK DKTE
//
