ID   CLPB_BORBR              Reviewed;         865 AA.
AC   Q7WHB6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=BB3293;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(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   ---------------------------------------------------------------------------
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; BX640447; CAE33785.1; -; Genomic_DNA.
DR   RefSeq; WP_003810451.1; NC_002927.3.
DR   AlphaFoldDB; Q7WHB6; -.
DR   SMR; Q7WHB6; -.
DR   STRING; 257310.BB3293; -.
DR   EnsemblBacteria; CAE33785; CAE33785; BB3293.
DR   GeneID; 56479407; -.
DR   KEGG; bbr:BB3293; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_4; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000001027; 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..865
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191095"
FT   DOMAIN          3..145
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          82..145
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          158..339
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          340..551
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          561..770
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          771..865
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          390..524
FT                   /evidence="ECO:0000250"
FT   BINDING         205..212
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   865 AA;  96376 MW;  CD15BE2D439DEA0C CRC64;
     MRFDKLTTKF QQALADAQSL AARNDHPYIE PVHVLAALLG DPDSGAASLL ARAGVAVNRV
     QPAIDSALKG LPQVQGEDNV QVGRELQSVL VRTDKEAARR GDTYIASELF LLALADDKGD
     AGRILREAGL QKKALEAAID AVRGGENVSG AEGESNREAL SKYTLDLTER ARQGKLDPVI
     GRDDEIRRTI QILQRRTKNN PVLIGEPGVG KTAIVEGLAQ RIVNDEVPET LRGKRVLSLD
     LAALLAGAKF RGEFEERLKA VLKELAQDDG QNIVFIDELH TMVGAGKAEG AMDAGNMLKP
     ALARGELHCI GATTLDEYRK YIEKDAALER RFQKVLVGEP DVESTIAILR GLQERYELHH
     GVEITDPAIV AAAELSHRYI TDRFLPDKAI DLIDEAGARI RMEIDSKPEV MDRLDRRIIQ
     LKIEREAVKK ETDDASMRRL AVIEEELEKL QREYNDYEEI WKAEKAAVQG TQAIKEEIDR
     VRAEMAELQR KGQFDKLAEL QYGKLPELEA RLKAADSAER EAGESDSGKP RLLRTQVGAE
     EIAEVVSRAT GIPVAKMMQG ERDKLLRMED FLHKRVVGQD EAVRLVSDAI RRSRAGLADP
     SRPYGSFLFL GPTGVGKTEL TRALADFLFD SEEHMIRIDM SEFMEKHSVA RLIGAPPGYV
     GYEEGGYLTE AVRRKPYSVI LLDEVEKAHP DVFNVLLQVL DDGRLTDGQG RTVDFRNTVI
     VMTSNLGSQH IQSMAGKPYE VIKEVVWDEL KHTFRPEFLN RIDEVVVFHG LEAQHIESIA
     RIQLKRLGER LEKQEMRLDV SDAALAEIAR SGFDPVFGAR PLKRAIQQQI ENPVAKLILE
     GVFGPRDVVP VDWQDGKFVF TRTLQ