ID   CLPB1_NOSS1             Reviewed;         880 AA.
AC   Q8YUL9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Chaperone protein ClpB 1;
GN   Name=clpB1; OrderedLocusNames=alr2322;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB74021.1; -; Genomic_DNA.
DR   PIR; AC2096; AC2096.
DR   RefSeq; WP_010996478.1; NZ_RSCN01000004.1.
DR   AlphaFoldDB; Q8YUL9; -.
DR   SMR; Q8YUL9; -.
DR   STRING; 103690.17131414; -.
DR   EnsemblBacteria; BAB74021; BAB74021; BAB74021.
DR   KEGG; ana:alr2322; -.
DR   eggNOG; COG0542; Bacteria.
DR   OMA; GPEHILM; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000002483; 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..880
FT                   /note="Chaperone protein ClpB 1"
FT                   /id="PRO_0000191085"
FT   DOMAIN          6..148
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          85..148
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          161..343
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          344..554
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          564..775
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          776..880
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          394..530
FT                   /evidence="ECO:0000250"
FT   BINDING         208..215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         614..621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   880 AA;  99047 MW;  6055268861E41794 CRC64;
     MQPTDPNKFT DKAWEVIVKS QDIVRAYQQQ QLDVEHLILA LIEDPTSLAV RILGRAEIDP
     IRLQQQLEAF TQRQTKVGKS DQLYLGRSLD VMLDRAEEIR ERMKDGYISV EHMLLAFVDD
     ERVGRKVLKG FNVDSAKIEA SIKAVRGSQK VTDQNPESRY EALQKFGRDL TEQAKSGKLD
     PVIGRDDEIR RVIQVLSRRS KNNPVLIGEP GVGKTAIAEA LAQRIVNGDV PESLKNRQLI
     SLDIGSLIAG AKYRGEFEDR LKAVLREVTE SNGNIVLFID ELHTVVGTGS NQQGAMDAGN
     LLKPMLARGE LRCIGATTLD EFRKFIEKDA ALERRFQQVY VDQPSVENTI SILRGLKERY
     EVHHNVKISD SALVAAATLS ARYIADRFLP DKAIDLVDEA AAQLKMEITS KPADLEAIDR
     RLMQLEMEKL SLAGEEKVAA PTKERLQRIE LEITNLTEKQ QDLNNQWQGE KQVLEAISLL
     KKEEDALRVQ IEQAERAYDL NKAAQLKYGK LEGVQRDREA KEAKLLELQS QGSTLLREQV
     TEADIAEIVA KWTGIPVNRL LESERQKLLQ LESHLHQRVI GQQEAVEAVS AAIRRARAGM
     KDPNRPIGSF LFMGPTGVGK TELARALAQF LFDADDALVR LDMSEYMEKH SVSRLVGAPP
     GYVGYEEGGQ LSEAVRRHPY SVVLLDEVEK AHPDVFNILL QVLDDGRITD SQGRTVDFRN
     TVIVMTSNIG SEHILDVSGD DTQYETMRNR VMDALRSHFR PEFLNRVDDT ILFHALSRSE
     MSHIIRIQLK RVESLLRDQK ISFEISPAAC DFLVEKGYDP VYGARPLKRA IQREIENPLA
     TKILENTFIS GDTIYIDQDE NGLSFTNKAP VKVSVTQITT