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 01-MAY-2013, entry version 64.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=BCE_1287;
OS Bacillus cereus (strain ATCC 10987).
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;
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
CC ATPase activity; ATP hydrolysis unfolds the denatured protein
CC aggregates, which probably helps expose new hydrophobic binding
CC sites on the surface of ClpB-bound aggregates, contributing to the
CC solubilization and refolding of denatured protein aggregates by
CC DnaK (By similarity).
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- DOMAIN: The N-terminal 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
CC stabilizes the hexamer probably in an ATP-dependent manner. The
CC movement of the coiled-coil domain is essential for ClpB ability
CC to rescue proteins from an aggregated state, probably by pulling
CC apart large aggregated proteins, which are bound between the
CC coiled-coils motifs of adjacent ClpB subunits in the functional
CC hexamer (By similarity).
CC -!- SIMILARITY: Belongs to the clpA/clpB family.
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DR EMBL; AE017194; AAS40216.1; -; Genomic_DNA.
DR RefSeq; NP_977608.1; NC_003909.8.
DR ProteinModelPortal; Q73BY1; -.
DR SMR; Q73BY1; 162-354.
DR STRING; 222523.BCE_1287; -.
DR PRIDE; Q73BY1; -.
DR EnsemblBacteria; AAS40216; AAS40216; BCE_1287.
DR GeneID; 2748015; -.
DR KEGG; bca:BCE_1287; -.
DR PATRIC; 18851438; VBIBacCer118379_1224.
DR eggNOG; COG0542; -.
DR HOGENOM; HOG000218209; -.
DR KO; K03695; -.
DR OMA; NIRDINA; -.
DR ProtClustDB; CLSK916118; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR GO; GO:0016485; P:protein processing; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR Gene3D; 1.10.1780.10; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013093; ATPase_AAA-2.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR018368; Chaperonin_ClpA/B_CS.
DR InterPro; IPR017730; Chaperonin_ClpB.
DR InterPro; IPR001270; Chaprnin_ClpA/B.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004176; Clp_N.
DR InterPro; IPR023150; Dbl_Clp-N.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 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 TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm;
KW Nucleotide-binding; Repeat; Stress response.
FT CHAIN 1 866 Chaperone protein ClpB.
FT /FTId=PRO_0000191089.
FT NP_BIND 209 216 ATP 1 (By similarity).
FT NP_BIND 611 618 ATP 2 (By similarity).
FT REGION 1 146 N-terminal (By similarity).
FT REGION 162 343 NBD1 (By similarity).
FT REGION 344 551 Linker (By similarity).
FT REGION 561 773 NBD2 (By similarity).
FT REGION 774 866 C-terminal (By similarity).
FT COILED 394 528 By similarity.
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
//
