GenomeNet

Database: UniProt
Entry: CLPB_BACC1
LinkDB: CLPB_BACC1
Original site: CLPB_BACC1 
ID   CLPB_BACC1              Reviewed;         866 AA.
AC   Q73BY1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=BCE_1287;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017194; AAS40216.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q73BY1; -.
DR   SMR; Q73BY1; -.
DR   KEGG; bca:BCE_1287; -.
DR   HOGENOM; CLU_005070_4_0_9; -.
DR   Proteomes; UP000002527; 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   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 78, MITOCHONDRIAL; 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; Repeat;
KW   Stress response.
FT   CHAIN           1..866
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191089"
FT   DOMAIN          3..149
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          86..149
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          162..343
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          344..551
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          561..773
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          774..866
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          394..528
FT                   /evidence="ECO:0000250"
FT   BINDING         209..216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         611..618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   866 AA;  97482 MW;  4BD1E18137CFE375 CRC64;
     MDLNQMTTKT QEAIMSAQSL AVSHHHQEVD TVHLLFTLLE EQDGLAVRIF QKMNVDIEAL
     KQGAEGLIKK KPSVTGSGAE AGKLYITGAL QQLLVRAGKE AEKLQDDYIS VEHVLLAFTE
     EKGDINQLFT RFHITKDNLL QSLMTVRGNQ RVTSQNPEAT YEALEKYGRD LVAEVRAGKI
     DPVIGRDSEI RRVIRILSRK TKNNPVLIGE PGVGKTAIVE GLAQRIVKKD VPEGLKDRTI
     FALDMSALVA GAKFRGEFEE RLQAVLNEIK KSEGRILLFI DELHTIVGAG KTEGAMDAGN
     MLKPMLARGE LHCIGATTLD EYRKYIEKDP ALERRFQQVL AEEPTVEDTI SILRGLKERF
     EIYHGVNIHD RAIVAASVLS DRYISDRFLP DKAIDLVDEA CATIRTEIDS MPTELDEVTR
     RIMQLEIEEA ALGKEKDFGS QERLKTLQRE LSDLKEVASG MRAKWEKEKE DIHKVRDLRE
     HLERLRRELE EAEGNYDLNK AAELRHGKIP AIEKELKEAE EMGAHNKQEN RLLREEVSEE
     EIADIVSRWT GIPVAKLVEG EREKLLRLEQ ILSERVIGQE EAVSLVSDAV LRARAGIKDP
     NRPIGSFIFL GPTGVGKTEL AKTLAQSLFD SEEQMIRIDM SEYMEKHAVS RLIGAPPGYV
     GYEEGGQLTE AVRRKPYSVI LLDEIEKAHP EVFNILLQML DDGRITDSQG RTVDFKNTVI
     IMTSNIGSAH LLDGLEDDGS IKEESRELVM GQLRGHFRPE FLNRVDEIIL FKPLTTNEIK
     GIVDKIVKEL QGRLADRHIT VELTDAAKEF VVEAGFDPMY GARPLKRYVQ RQVETKLARE
     LIASTITDNS HVVVDVENNE LVVHVK
//
DBGET integrated database retrieval system