CLPB_DEIRA
ID CLPB_DEIRA Reviewed; 852 AA.
AC Q9RVI3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=DR_1046;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF10620.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000513; AAF10620.1; ALT_INIT; Genomic_DNA.
DR PIR; G75442; G75442.
DR RefSeq; NP_294770.1; NC_001263.1.
DR RefSeq; WP_027479647.1; NC_001263.1.
DR AlphaFoldDB; Q9RVI3; -.
DR SMR; Q9RVI3; -.
DR STRING; 243230.DR_1046; -.
DR PRIDE; Q9RVI3; -.
DR EnsemblBacteria; AAF10620; AAF10620; DR_1046.
DR KEGG; dra:DR_1046; -.
DR PATRIC; fig|243230.17.peg.1242; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_0; -.
DR InParanoid; Q9RVI3; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000002524; Chromosome I.
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 GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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 TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
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; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..852
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191118"
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..69
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 81..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 151..331
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 332..535
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 545..756
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 757..852
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 382..513
FT /evidence="ECO:0000250"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 595..602
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 852 AA; 94878 MW; 2083AC118B7ABC02 CRC64;
MNPERFTEAS AVAINAAQQL AQENHNQNLT HFHVLRTLLD NDTASRALTL AGGDLNTARA
ALDAEIAKLP KVQGSDGQLY LDPALNRAFQ KADTLAAQLG DSFVAADTLL LALRGEYRGR
GLPDEVSLNR AVTEQRKGKT VTNKTSEQQF DALNKYGTDL TQRARDGKFD PVIGRDEEIR
RVMQILLRRS KNNPVLIGEP GVGKTAIAEG LAMRIVKGDV PEGLRDKKIV SLEMGSLLAG
AKFRGEFEER LKGVIDEVVK SAGEIILFVD EIHTIVGAGK TEGSPDAGNM LKPALARGEL
HLIGATTLDE YREIEKDAAL ERRFQPVFVD EPSVEDTISI LRGIKERYQV HHNVEITDPA
LVAAATLSNR YITDRQLPDK AIDLIDESAA RLRMALESSP ERIDQLSRRK LQLEIEREAL
KREKDVDSQN RLLDIENQLK TLTDELNEVR SRWEAERGEV AALREKREKL DAVRTQIEKA
RRDYDLEEAA RLEYGELPAL EKDVQDLEKK LKSAEFAHME VTEEDIAAVV SRWTGIPVSK
LMEGEREKLL HLEEQLHGRV IGQDRAIVSV SDAIRRARAG LNDPNRPLGS FMFLGPSGVG
KTELAKALAE FLFDSSDAMV RIDMSEYMEK HTVARLIGAP PGYVGFEEGG QLTEAVRRRP
YAVILFDEIE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFR NTLIIMTSNI GSPLILEMQQ
RGEDAETIKS AVMDELRGEF RPEFLNRVDD IIVFDALTAK DLQSIVDIQL GGLRRRLAER
RITLHLTEDA KDKLAELGYD PAYGARPLRR TISQYIETPL AREILGGQIQ DGSVLNVDYG
DGGFTFNSGS LN
