ID   CLPB_STAAS              Reviewed;         869 AA.
AC   Q6GAV1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=SAS0845;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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}.
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DR   EMBL; BX571857; CAG42620.1; -; Genomic_DNA.
DR   RefSeq; WP_000353955.1; NC_002953.3.
DR   AlphaFoldDB; Q6GAV1; -.
DR   SMR; Q6GAV1; -.
DR   KEGG; sas:SAS0845; -.
DR   HOGENOM; CLU_005070_4_0_9; -.
DR   OMA; GPEHILM; -.
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..869
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191179"
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          85..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..549
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          559..771
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          772..869
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         609..616
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   869 AA;  98303 MW;  72B80D8A24DFF4A3 CRC64;
     MDINKMTYAV QSALQQAVEL SQQHKLQNIE IEAILSAALN ESESLYKSIL ERANIEVDQL
     NKAYEDKLNT YASVEGDNIQ YGQYISQQAN QLITKAESYM KEYEDEYISM EHILRSAMDI
     DQTTKHYINN KVEVIKEIIK KVRGGNHVTS QNPEVNYEAL AKYGRDLVEE VRQGKMDPVI
     GRDEEIRNTI RILSRKTKNN PVLIGEPGVG KTAIVEGLAQ RIVKKDVPES LLDKTVFELD
     LSALVAGAKY RGEFEERLKA VLKEVKESDG RIILFIDEIH MLVGAGKTDG AMDAGNMLKP
     MLARGELHCI GATTLNEYRE YIEKDSALER RFQKVAVSEP DVEDTISILR GLKERYEVYH
     GVRIQDRALV AAAELSDRYI TDRFLPDKAI DLVDQACATI RTEMGSNPTE LDQVNRRVMQ
     LEIEESALKN ESDNASKQRL QELQEELANE KEKQAALQSR VESEKEKIAN LQEKRAQLDE
     SRQALEDAQT NNNLEKAAEL QYGTIPQLEK ELRELEDNFQ DEQGEDTDRM IREVVTDEEI
     GDIVSQWTGI PVSKLVETER EKLLHLSDIL HKRVVGQDKA VDLVSDAVVR ARAGIKDPNR
     PIGSFLFLGP TGVGKTELAK SLAASLFDSE KHMIRIDMSE YMEKHAVSRL IGAPPGYIGH
     DEGGQLTEAV RRNPYSVILL DEVEKAHTDV FNVLLQILDE GRLTDSKGRS VDFKNTIIIM
     TSNIGSQVLL ENVKETGEIT ESTEKAVMTS LNAYFKPEIL NRMDDIVLFK PLSIDDMSMI
     VDKILTQLNI RLLEQRISIE VSDDAKAWLG QEAYEPQYGA RPLKRFVQRQ IETPLARMMI
     KEGFPEGTTI KVNLNSDNNL TFNVEKIHE