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 03-AUG-2022, entry version 102.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=BCE_1287;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; 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 RefSeq; WP_000365369.1; NC_003909.8.
DR AlphaFoldDB; Q73BY1; -.
DR SMR; Q73BY1; -.
DR PRIDE; Q73BY1; -.
DR EnsemblBacteria; AAS40216; AAS40216; BCE_1287.
DR GeneID; 59158992; -.
DR KEGG; bca:BCE_1287; -.
DR HOGENOM; CLU_005070_4_0_9; -.
DR OMA; GPEHILM; -.
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 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..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
