ID   CLPB_WOLSU              Reviewed;         857 AA.
AC   Q7M9X4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=WS0609;
OS   Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS   11488 / FDC 602W) (Vibrio succinogenes).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Wolinella.
OX   NCBI_TaxID=273121;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC   11488 / FDC 602W;
RX   PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA   Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA   Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA   Meyer F., Lederer H., Schuster S.C.;
RT   "Complete genome sequence and analysis of Wolinella succinogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(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; BX571658; CAE09740.1; -; Genomic_DNA.
DR   RefSeq; WP_011138540.1; NC_005090.1.
DR   AlphaFoldDB; Q7M9X4; -.
DR   SMR; Q7M9X4; -.
DR   STRING; 273121.WS0609; -.
DR   EnsemblBacteria; CAE09740; CAE09740; WS0609.
DR   KEGG; wsu:WS0609; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_7; -.
DR   OMA; KRYITDH; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000000422; 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; -; 3.
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   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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; Repeat; Stress response.
FT   CHAIN           1..857
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191205"
FT   DOMAIN          4..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          7..72
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          85..146
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          159..339
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          340..548
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          558..765
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          766..857
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          390..525
FT                   /evidence="ECO:0000250"
FT   BINDING         206..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         608..615
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   857 AA;  96108 MW;  E68331DB14E39B74 CRC64;
     MNAFEKMTHQ LRETLEQALS LALHAKNPEV DLPHMAWALL INSTSILNQA LNKMGVDKSA
     LELEAKSLVD RLPQSSSLTK ENIKISKRLA DSLTQAEALG VKGGDKFIAV DTWLLANLKE
     EPLKSLFSKY LDVNELKKNL ESIRGGAKIE SATDDENLES LAKYGIDLTQ KALENKLDPV
     IGRDEEISRM MQILIRKTKN NPILLGEPGV GKTAVVEGLA QRIIAKEVPL SLQNKRVVAL
     DMSALIAGAK YRGEFEDRLK KVVEEVKKAG NVILFIDEIH TIVGAGASEG SMDAANILKP
     ALARGELHTI GATTLKEYRK YFEKDAALQR RFQPIFLNEP TINEALQILR GIKERLEAHH
     NVTIYDSALV AAAKLSSRYI TDRYLPDKAI DLIDEAAAEL KMQIESEPTE LSLIKRQIQR
     LEVEKEALLM EKESTHSEAR IKEIQAELEN AKERQRTLLA QFENEKAVFN EIASIKAKAD
     ELRRESELAK RSGDYNKAAE IDYGKIPELE NREKELNTQW NRMQESGTLL KNAVSEESIA
     GIVSRWTQIP VKKMLQGEKE KVLGVEEELR KDVVGQDEAL HAIARAIKRN KAGLSENNRP
     IGSFLFLGPT GVGKTQSAKT LAKFLFDSDK NLVRIDMSEY MEKHAASRLV GAPPGYVGYE
     EGGQLTEAIR RKPYSVVLFD EIEKAHPDVF NILLQVLDDG RLTDNKGVTV DFRNTIIILT
     SNIASDKIME NSDKERRESA VKAELKRYFK PEFLNRLDDI IIFNPLGLAQ IVEIVEIMFE
     GIREKLKERQ ITLELTQSAK EQIAEVGFDP VYGARPLKRA LYEEVEDRLA ELILEDKISE
     GSHVVFDAQG GKIIARI