ID   CLPB_OCEIH              Reviewed;         809 AA.
AC   Q8EU05;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=OB0093;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC12049.1; -; Genomic_DNA.
DR   RefSeq; WP_011064496.1; NC_004193.1.
DR   AlphaFoldDB; Q8EU05; -.
DR   SMR; Q8EU05; -.
DR   STRING; 221109.22775771; -.
DR   EnsemblBacteria; BAC12049; BAC12049; BAC12049.
DR   KEGG; oih:OB0093; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   PhylomeDB; Q8EU05; -.
DR   Proteomes; UP000000822; 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   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; 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   InterPro; IPR001943; UVR_dom.
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   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; Repeat; Stress response.
FT   CHAIN           1..809
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191150"
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   DOMAIN          420..455
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT   REGION          6..71
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          80..144
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          145..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..344
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          345..488
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          498..716
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          717..809
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          395..471
FT                   /evidence="ECO:0000250"
FT   BINDING         211..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         548..555
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   809 AA;  90503 MW;  4257E790A0B06B7B CRC64;
     MMFGRFTERA QKVLALSQEE AVRLGHNNIG TEHILLGLVR EGEGIAAKAL QSLGLEVSKI
     QEEVEKLIGV GKQPTQSIHY TPRAKKVVEL SQDEARKLGH SYVGTEHILL GLIREGEGVA
     ARVLNNLGVS LNKARQQVLQ LLGSNESQAG RQGRSGQQSN ASTPTLDSLA RDLTVSAKEG
     KIDPVIGRSK EIERVIQVLS RRTKNNPVLI GEPGVGKTAV AEGLAQQIID NEVPETLRDK
     RVMTLDMGTV VAGTKYRGEF EDRLKKVMEE IRQAGNIILF IDELHTLIGA GGAEGAIDAS
     NILKPSLARG ELQCIGATTL DEYRKYIEKD AALERRFQPI QVDEPTLEET IQILNGLRDR
     YEAHHRVTIT DEAIEAAASL SDRYITDRFL PDKAIDLIDE AGSKVRLRSY TVPPNLKELE
     QKLDEVRKEK DAAVQSQEFE KAASLRDSEQ RFREELETTK NQWKEKQGQT DSEVTMEDIA
     AVVSTWTGVP VSKLTKDETD RLLNMEKILH DRVIGQSEAV NAVAKAIRRA RAGLKDPKRP
     IGSFIFLGPT GVGKTELARA LAEVMFADED AMIRIDMSEY MERHATSRLV GSPPGYVGYD
     EGGQLTEKVR RKPYSVVLLD EVEKAHPEVF NILLQVLEDG RLTDSKGRVV DFRNTVIIMT
     SNVGASELKR NKYVGFALDN EEKDYKDMKS KVIEELKKAF RPEFLNRIDE TIVFHSLEKE
     HMKDIVTLMV QQLQKRLKEQ DLHLSLTDKA IEKIANEGFD PEYGARPLRR SIQKNIEDLL
     SEELLRGAIE KEQQVKIGLN NKGEFIVLP