CLPB_AQUAE
ID CLPB_AQUAE Reviewed; 1006 AA.
AC O67588;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=aq_1672;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The Clp repeat (R) domain probably functions as a substrate-
CC discriminating domain, recruiting aggregated proteins to the ClpB
CC hexamer and/or stabilizing bound proteins. The NBD2 domain is
CC responsible for oligomerization, whereas the NBD1 domain stabilizes the
CC hexamer probably in an ATP-dependent manner. The movement of the
CC coiled-coil domain is essential for ClpB ability to rescue proteins
CC from an aggregated state, probably by pulling apart large aggregated
CC proteins, which are bound between the coiled-coils motifs of adjacent
CC ClpB subunits in the functional hexamer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07550.1; -; Genomic_DNA.
DR PIR; C70445; C70445.
DR RefSeq; NP_214154.1; NC_000918.1.
DR RefSeq; WP_010881091.1; NC_000918.1.
DR AlphaFoldDB; O67588; -.
DR SMR; O67588; -.
DR STRING; 224324.aq_1672; -.
DR PRIDE; O67588; -.
DR EnsemblBacteria; AAC07550; AAC07550; aq_1672.
DR KEGG; aae:aq_1672; -.
DR PATRIC; fig|224324.8.peg.1295; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_0; -.
DR InParanoid; O67588; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR Gene3D; 1.10.1780.10; -; 2.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
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 InterPro; IPR001943; UVR_dom.
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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..1006
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191087"
FT DOMAIN 3..289
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT DOMAIN 603..638
FT /note="UVR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT REGION 7..72
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 225..289
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 251..473
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 474..666
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 676..893
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 894..1006
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 524..648
FT /evidence="ECO:0000250"
FT BINDING 340..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 726..733
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1006 AA; 114537 MW; FEBB850E75D1A8EF CRC64;
MISENLFSAK SLEYLEKAKE IARENKDTKV DTDHLLIALL LDEKSPLSKY IEKRGIDRKE
FLKRVSEYLE NLNKQLEKAI EAEAQNLINL RTQIMEVKSN IGNVQTELSK IRKAKERILR
ELEYARRYGD WWTAETLELE LRQLEATEQS IRRQLEQVEK SLSTVFAPED VKAFLENKLS
IDGLIRKALE KSPLIEQVKE LGISPDRIID KVAEKVFGKK PTFDYSQYLT QVLEKAQDKA
VSEGEAQVQP SHISAALIEA KDTIGGKLIN QVLGGEKEMK KDVTQELKEE EKSPLERFGV
NLNELARQGK LDPVIGRERE INQVIEILLR RTKNNPVLVG DPGVGKTAIV EGLAQRIVNK
EVPPELQDKE IWSIDMASLL AGSKYRGEFE ERLKALLDEV KEKGNVILFI DEIHTVVGAG
AAEGAVDAAN IMKPALARGE IRVIGATTVD EYRKYIEKDP ALERRFQPVF VDEPTEEQTI
EILKGLRPRL EQFHKVKISD EAIEAAVKLT KRYVTFRRLP DKAIDALDQA AARKKLKVIG
TPPEIQEIER KIKALEEQII EANLKGDYEK EAQLKIEKAK LEKEKQELLG KVGGVEAKIA
ELKKKIEELD EKIKEAAEKG DYEKEAELKI EKAKLEKELK KLEQEKSKEL VVTWDDVAEV
VSEWTGIPVS RLKEEEMQKL LKLEDELHKR VVDQEHAVKA VAEAIRRARA GLKDPKRPIA
SFLFLGPTGV GKTELSKALA ELLFGDEDAL IRLDMSEFKE EHSVAKLIGA PPGYVGYEEG
GKLTEAVRRK PYSVILLDEI EKAHPRVLDL FLQVLDDGRL TDSHGRTVDF RNTVIIMTSN
IGSQYLLNIP VDADEETLNR EFEKAKEKVL EELKLYMRPE FINRIDEIIV FKPLTMRELS
KIIDLLIANV NKRLAERNIK IELTEEAKKE LVRRGYDPAF GARPLKRTIQ KYVETPLADK
IIRGEIKDGM TVVVDYKDGE FVFIPKEEYE KQKAEVSASS EEKKES
