CLPB_RALSO
ID CLPB_RALSO Reviewed; 862 AA.
AC Q8XZR0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=RSc1335; ORFNames=RS02857;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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; AL646052; CAD15037.1; -; Genomic_DNA.
DR RefSeq; WP_011001284.1; NC_003295.1.
DR AlphaFoldDB; Q8XZR0; -.
DR SMR; Q8XZR0; -.
DR STRING; 267608.RSc1335; -.
DR PRIDE; Q8XZR0; -.
DR EnsemblBacteria; CAD15037; CAD15037; RSc1335.
DR GeneID; 60500857; -.
DR KEGG; rso:RSc1335; -.
DR PATRIC; fig|267608.8.peg.1360; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_4; -.
DR OMA; SKMMQGE; -.
DR Proteomes; UP000001436; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; 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..862
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191164"
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..71
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 82..145
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 158..339
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 340..548
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 558..767
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 768..862
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 390..524
FT /evidence="ECO:0000250"
FT BINDING 205..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 608..615
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 862 AA; 95559 MW; 52D987533842EC29 CRC64;
MRLDKLTTRF QEALADAQSL ALGNDNPYIE PLHLLLAMLR QPDGATKNLL ARAGVNAKGL
EIALDNAIKR LPQVQGGEQV QVGRDLGSLL QATEKEGIKR GDQFIASELF LLAVADDKGE
AGRVAREHGL ARRALEAAID AVRGGQTVGS AEAESQREAL KKYTIDLTEQ ARIGKLDPVI
GRDDEIRRAI QILQRRTKNN PVLIGEPGVG KTAIVEGLAQ RIINGEVPES LKNKRVLVLD
MAGLLAGAKY RGEFEERLKA VLNDIAKEEG QTILFIDEIH TMVGAGKAEG AIDAGNMLKP
ALARGELHCI GATTLDEYRK YIEKDAALER RFQKVLVDEP SVEATIAILR GLQEKYELHH
GVEITDPAIV AAAELSHRYI TDRFLPDKAI DLIDEAAARI KMEIDSKPEA MDKLDRRLIQ
LKIEREAVKK ETDEASQKRL ELIEQEIERL QKEYADLEEI WKAEKGAAQG AAAVKEEIDR
VKLEIARLQR EGKLDKVAEL QYGRLPELEG KLKAATAAEA SGQRPPNKLL RTQVGAEEIA
EVVSRATGIP VSKMMQGERD KLLRMEDRLH ERVVGQDEAV RLVSDAIRRS RAGIADENKP
YGSFLFLGPT GVGKTELCKA LAGFLFDSEE HLIRIDMSEF MEKHSVSRLI GAPPGYVGYE
EGGYLTEAVR RKPYSVVLLD EVEKAHPDVF NILLQVLDDG RLTDGQGRTV DFKNTVIVMT
SNLGSQLIQQ MASESPDVIK GAVWQEVKTH FRPEFLNRID EVVVFHALDQ GHIESIARIQ
LQRLAARLAH MDLTLEISDP AVAKLASAGY DPVFGARPLK RAIQQQIENP VARMILEGRF
TPKDVVPVDY HDGHFTFDRV VR
