CLPB_RICTY
ID CLPB_RICTY Reviewed; 858 AA.
AC Q68XR2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=RT0094;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03580.1; -; Genomic_DNA.
DR RefSeq; WP_011190567.1; NC_006142.1.
DR AlphaFoldDB; Q68XR2; -.
DR SMR; Q68XR2; -.
DR STRING; 257363.RT0094; -.
DR PRIDE; Q68XR2; -.
DR EnsemblBacteria; AAU03580; AAU03580; RT0094.
DR KEGG; rty:RT0094; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_5; -.
DR OMA; ERMKAVM; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000000604; 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..858
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000281062"
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..858
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 858 AA; 96288 MW; 5F979124653DDEFB CRC64;
MNIDKFTAHA KSVIANHQSL AIKNDHQQIL PLHLLSSLLS EETGIIQALI NNIGGNIHLL
KDQVQLELNK IPKIQVDGGG QIYYSAEDLK VLEKSRSIAK DSGDSFVTIE RIFEALTYDN
TIAGKILTNN GINSKKLAAA ILHLRKGKKA DTESAENSYD ALKRYGRDVT ELAKNGKLDP
IIGRDEEIRR AVQVLSRRMK NNPVLIGAPG VGKTAIIEGL AQRIFNKDVP ETLINCRIIE
LDIGALIAGA QYRGEFEKRL KSVLSEIKES SGEIILFIDE LHLLVGTGKV EGAMDASNLL
KPMLARGELH CIGATTLDEY RKYIEKDAAL ARRFQPVYVG EPSVEDTISI LRGIKEKYEL
HHAVRISDSA IVAAATLSNR YITDRYLPDK AIDLIDEACS RMKIELSSKP EELDELDRRI
IQIKIELAAL KKENDEHSKK KITSLTEELK QLDSKSYDMN TKWQAAKSKL QQAQKLKEEL
EQARIDLDRA ERDANLAKAS ELKYGIIPEI MNKLQAAENM DNKGLLKEIV SESDIASIIS
RITGIPIDTM LSSERERLLV IEQKLSESVI GQDEAIKGIS DAVRRSRSGI QDINRPLGSF
LFLGPTGVGK TELTKALAGF LFDDRNALLR IDMSEYMEKH SISRLIGAPP GYIGYDQGGV
LTESVRRRPY QVILFDEVEK AHLDIFNIML QILDEGRLTN SQGITVDFKN TIIVLTSNLG
AEILVNQQED EDTYKVKDEV MQYVRAVFKP EFLNRLDEII LFHRLNRNNI YDIVKIQLGS
LKKILLQQNI ILEFNESALN YLAEKGYDPS FGARPLKRLI QREIQNNLAK MILAGKISSG
NTVKIAREKE ELRIEIID
