ID   CLPB_CLOTE              Reviewed;         865 AA.
AC   Q898C7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=CTC_00536;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(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}.
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DR   EMBL; AE015927; AAO35156.1; -; Genomic_DNA.
DR   RefSeq; WP_011098823.1; NC_004557.1.
DR   AlphaFoldDB; Q898C7; -.
DR   SMR; Q898C7; -.
DR   STRING; 212717.CTC_00536; -.
DR   PRIDE; Q898C7; -.
DR   EnsemblBacteria; AAO35156; AAO35156; CTC_00536.
DR   GeneID; 64180386; -.
DR   KEGG; ctc:CTC_00536; -.
DR   HOGENOM; CLU_005070_4_0_9; -.
DR   OMA; GPEHILM; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000001412; 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;
KW   Reference proteome; Repeat; Stress response.
FT   CHAIN           1..865
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191113"
FT   DOMAIN          3..150
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          86..150
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          163..344
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          345..551
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          561..772
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          773..865
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          395..529
FT                   /evidence="ECO:0000250"
FT   BINDING         210..217
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;  98580 MW;  79867BE7FCE4CBB0 CRC64;
     MDIEKLTLKV QQTINDSQKI AVKYNHQQLE PFHLFAALVF QEDGLIPNIL GKMNINIKVL
     RDEIKRELNE MPKVLGDGAQ NSGVYATRSF EEIFIRAESI AKDFKDSYIS VEHIMLSLMQ
     GRSTSIKKIL DKFNIRKDKF LNVLQQVRGN QRVDTQDPEG TYEALVKYGR NLIEDAKKHK
     LDPVIGRDEE IRRIVRILSR RTKNNPVLIG DPGVGKTAII EGLAERIVRG DVPEGLKNKI
     IFSLDMGALI AGAKFRGEFE ERLKAVLKEV ENSQGKIILF IDEIHNIVGA GKTEGSMDAG
     NLIKPMLARG ELNCIGATTF DEYRKYIEKD KALERRFQPV IIDEPTVEDT ISIIRGLKER
     FEIHHGIRIH DSAIVAAAKL SQRYITDRYL PDKAIDLIDE AGAMIRTEID SLPTELDSIK
     RKIFQMEIEK EALAKEKDSR SKERLEDLEK ELSNLKEKDK EMTAKYEKEK EQIINMRNLK
     QKLDEVKGQL EKAEREYDLN KVAELKYGII PGIKSQIEEK EILIKENSQG NMLKEEVTEN
     EISKIISHWT GIPVTKLIEG EKDKLLRLED ELKSRVIGQD EAVEAVSNAV LRARAGMKDP
     QKPIGSFIFL GPTGVGKTEL AKTLCKNLFD SEENIIRIDM SEYMEKYSVS RLIGAPPGYV
     GYEEGGQLTE AVRRKPYSVI LFDEIEKAHD DVFNIFLQIL DDGRLTDNKG KTVDFKNCII
     IMTSNIGSSY LLENKKEDGI DETVKNKVSN ALKDRFKPEF LNRLDDIIMF KPLTNREITK
     IIDIFLQDIE NRLKDRNITL IVTENAKELM AKEGYDAIYG ARPLKRYIEN ILETKIAKQI
     IKGDIYEGCK IGVDIKGEEI IIGKI