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Database: UniProt
Entry: CLPB_RHOBA
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Original site: 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   13-SEP-2023, entry version 101.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=RB9103;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; 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   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; 9803641at2; -.
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   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
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; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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
//
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