ID   CLPB_GLOVI              Reviewed;         872 AA.
AC   Q7NFE9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=gll3577;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(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; BA000045; BAC91518.1; -; Genomic_DNA.
DR   RefSeq; NP_926523.1; NC_005125.1.
DR   RefSeq; WP_011143566.1; NC_005125.1.
DR   AlphaFoldDB; Q7NFE9; -.
DR   SMR; Q7NFE9; -.
DR   STRING; 251221.35214149; -.
DR   PRIDE; Q7NFE9; -.
DR   EnsemblBacteria; BAC91518; BAC91518; BAC91518.
DR   KEGG; gvi:gll3577; -.
DR   PATRIC; fig|251221.4.peg.3610; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_3; -.
DR   InParanoid; Q7NFE9; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   PhylomeDB; Q7NFE9; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; 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..872
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191125"
FT   DOMAIN          6..149
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          9..74
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          86..149
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          162..343
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          344..552
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          562..773
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          774..872
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          394..528
FT                   /evidence="ECO:0000250"
FT   BINDING         209..216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         612..619
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   872 AA;  98199 MW;  8538EE704B9C8230 CRC64;
     MQPNNPNQFT EKAWDAIVRT TEVAKEYRQQ QLESEHLFKA LLDQDGGLAG SIFTKAGVNL
     TKLGERVEQF INRQPKLTNP GQSVYLGRSL DALLDRAEGF RKEYGDDFIS IEHLVLAFAK
     DVRFGQQILR EFSLDEAKLK AVVAQVRGNQ KVTSQNPEST YESLDKYGRD LTQLAREGKL
     DPVIGRDEEI RRTIQILSRR TKNNPVLIGE PGVGKTAIAE GLAQRIVSGD VPESLQGRKL
     IALDMGALIA GSKYRGEFEE RLKAVLNEVT KSEGQIVLFI DEIHTVVGAG ATQGAMDAGN
     LLKPMLARGE LRCIGATTLD EYRKYIEKDA ALERRFQQVY VDQPTVEDTI SILRGLKERY
     EVHHGVRISD SALVAAAVLS HRYISDRFLP DKAIDLMDEA AAKLKMEITS KPEALDEVDR
     KILQLEMERL SLAKESDAAS RDRLERLEKE LADLKEEQRS LNAQWQAEKD IIDQVQAVKE
     EIDQVNVQIQ QAERDYDLNR AAELKYGKLS ELQKRLDAAD KQLSETQTSG RSLLREEVTE
     EDIAEIISKW TGIPVSKLVA SEREKLLHLE DELHKRVVGQ EEAVRIVSEA IQRSRAGLAD
     PNRPIASFIF LGPTGVGKTE LAKALASFLF DDENAMVRID MSEYMEKHSV SRLIGAPPGY
     VGYDEGGQLT EAVRRRPYAV VLFDEIEKAH NDVFNVLLQV LDDGRITDSQ GRTIDFKNAV
     IIMTSNIGSD AILRLGGNDA YYEQMREEVM RAMQVHFRPE FLNRVDDIII FRNLRRDQLA
     AIVKLQIARL EKRLADRKIT LKLSEAAIDY IVEAGYDPVY GARPLKRAIQ NELVNPLARG
     LLKGDFNDGD TIFVDIENER PVFRRLSAMP VV