GenomeNet

Database: UniProt
Entry: Q73BY1
LinkDB: Q73BY1
Original site: Q73BY1 
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   29-OCT-2014, entry version 72.
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). {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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; EKAVMDS; -.
DR   OrthoDB; EOG65F8SM; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017730; Chaperonin_ClpB.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004176; Clp_N.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR023150; Dbl_Clp-N.
DR   InterPro; IPR027417; P-loop_NTPase.
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   SUPFAM; SSF52540; SSF52540; 2.
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. {ECO:0000250}.
FT   NP_BIND     611    618       ATP 2. {ECO:0000250}.
FT   REGION        1    146       N-terminal. {ECO:0000250}.
FT   REGION      162    343       NBD1. {ECO:0000250}.
FT   REGION      344    551       Linker. {ECO:0000250}.
FT   REGION      561    773       NBD2. {ECO:0000250}.
FT   REGION      774    866       C-terminal. {ECO:0000250}.
FT   COILED      394    528       {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