CLPB_RHOBA
ID CLPB_RHOBA Reviewed; 881 AA.
AC Q7UM33;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=RB9103;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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=CAD76084.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX294148; CAD76084.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_868707.1; NC_005027.1.
DR AlphaFoldDB; Q7UM33; -.
DR SMR; Q7UM33; -.
DR STRING; 243090.RB9103; -.
DR PRIDE; Q7UM33; -.
DR EnsemblBacteria; CAD76084; CAD76084; RB9103.
DR KEGG; rba:RB9103; -.
DR PATRIC; fig|243090.15.peg.4362; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_0; -.
DR InParanoid; Q7UM33; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000001025; 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 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..881
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191167"
FT DOMAIN 5..147
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 8..73
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..568
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 528..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..789
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 790..881
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 392..530
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 628..635
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 881 AA; 97443 MW; B1B09910EB4E36C7 CRC64;
MAFRIDKLTT QAQNVVAEAQ AQATSAGNAE IDPLHVLSAA VNQRDGITTP LLEKINVDVP
KLKSLLTSEL EKLPHASGMG QARVSAKLQA ALEASATSAE SLKDEYVSTE HLLVGLARTD
NKAKNLLSLL GVSDNDLLTA MSQIRGSARV TDPNAESTYQ ALEKFGIDLT QLAQSGKLDP
VIGRDNEIRR VIQVLSRRTK NNPVLIGQPG VGKTAIAEGL ALRIFEGDVP QSLKGKKVVS
LDMGALVAGA KFRGDFEERL KSVLREVKDS DGKVILFIDE LHLVVGAGNA EGSADAANLL
KPELARGALR CIGATTLDEY RQHIEKDAAL ERRFQPVFVG EPNVEDTVAI LRGLKPRYES
HHGVRITDSA LVAAANLSDR YIADRFLPDK AIDLIDEAAS RLAMEKESVP EPIDRLQRRL
RQLELVHRQL VDEQEASAVD KRVEVEEEME SAKAELASLK EQWETEKMGL DDVQSVRQEV
DQLQHRFAQL DADAKEKQLR GESPEDAYSE MLQVQSRLRE LQARIDEAEK HDDSADQTKE
EPGDEKRRLL RKEVTEEEIA EVVSTWTGVP VTRMMETERA KLLVMEERLH QRVVGQDEAV
TAVSDAVRRS RSGLQDPNRP IGSFLFLGPT GVGKTELCKA LAEVMFDDES AMVRIDMSEF
MERHSVSRLI GAPPGYVGYE EGGKLTEAVR RRPYAVILLD EMEKAHPDVF NVLLQVLDDG
RLTDGQGRTV NFTNTVVVMT SNVGSQVIQR VTEEGGGEDE MRQAVEDALK ARFLPEFLNR
IDDTVIFHPL QQTQIRRIVQ LQLEELRSRL AANGLSFEIT DAAIDQIAEV GYDPAYGARP
LKRVIQREVQ NPLASAILKN SYAEGTTIKI DHDGDQFVFS G
