CLPB_RICCN
ID CLPB_RICCN Reviewed; 857 AA.
AC Q92JK8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=RC0059;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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; AE006914; AAL02597.1; -; Genomic_DNA.
DR PIR; C97707; C97707.
DR RefSeq; WP_010976745.1; NC_003103.1.
DR AlphaFoldDB; Q92JK8; -.
DR SMR; Q92JK8; -.
DR PRIDE; Q92JK8; -.
DR EnsemblBacteria; AAL02597; AAL02597; RC0059.
DR KEGG; rco:RC0059; -.
DR PATRIC; fig|272944.4.peg.70; -.
DR HOGENOM; CLU_005070_4_0_5; -.
DR OMA; ERMKAVM; -.
DR Proteomes; UP000000816; 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; Repeat;
KW Stress response.
FT CHAIN 1..857
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191169"
FT DOMAIN 3..147
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 84..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 160..341
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 342..544
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 554..764
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 765..857
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 392..523
FT /evidence="ECO:0000250"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 604..611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 857 AA; 95972 MW; 2D34E3A0BCE47C8A CRC64;
MNIDKFTAHA KSVIASSQLL AAKNDHQQIL PLHLLSSLLS EETGIIQTLI NNTGGNINLL
KDQVQLELNK IPKVQVEGGG QVYSSAEALK VLEKASSIAK DNGDSFVTIE RIFEALTYDN
TIAGKILTNN GINNKKIATA ILQFRKGKKA DTESAENSYD ALKKYGRDVT ELAESGKLDP
IIGRDEEIRR TVQVLSRRMK NNPVLIGEPG VGKTAIIEGL AQRIFSKDVP ESLINCRIIE
LDMGALIAGA KYRGEFEERL KAVLSEIKES SGEIILFIDE LHLLVGTGKT DGAMDASNLL
KPMLARGELH CIGATTLDEY RKYIEKDAAL ARRFQPVYVS EPTVEDTISI LRGIKEKYEL
HHAVRISDSA IVAAATLSNR YITDRYLPDK AIDLIDEACS RMKIELSSKP EELDELDRRI
IQIKIELAAL KKENDEHSKK KIEHLTTALE KLESQSYDMG AKWQAEKSKL QQTQKLKEEL
DRSRNELERA ERDANLAKAS ELKYGIIPEI MKKLQEAESM DNKGLLKEIV SESDIASIIS
RITGIPIDTM LSSERERLLV MEQKLRESVI GQDKAIKGVS DAVRRSRAGI QDINRPLGSF
LFLGPTGVGK TELTKALAGF LFDDRNAILR IDMSEYMEKH AISRLIGAPP GYIGYDQGGV
LTEAVRRRPY QVILFDEVEK AHPDIFNIML QILDEGRLTD SQGITVDFKN TIIVLTSNLG
AEILVNQKED EDTYKVKDEV MEYVKAVFKP EFLNRLDEII LFHRLNRNNI HDIVKIQLES
LKKILLAQNI ILEFDESALN YLAEKGYDPS FGARPLKRLI QREIQNNLAK MILAGEISSG
KTVKINSKDK ELKVTMS
