ID   CLPB2_NOSS1             Reviewed;         872 AA.
AC   Q8YM56;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Chaperone protein ClpB 2;
GN   Name=clpB2; OrderedLocusNames=alr5084;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB76783.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000019; BAB76783.1; ALT_INIT; Genomic_DNA.
DR   PIR; AD2441; AD2441.
DR   RefSeq; WP_044522472.1; NZ_RSCN01000014.1.
DR   AlphaFoldDB; Q8YM56; -.
DR   SMR; Q8YM56; -.
DR   STRING; 103690.17134222; -.
DR   PRIDE; Q8YM56; -.
DR   EnsemblBacteria; BAB76783; BAB76783; BAB76783.
DR   KEGG; ana:alr5084; -.
DR   eggNOG; COG0542; Bacteria.
DR   OMA; SKMMQGE; -.
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..872
FT                   /note="Chaperone protein ClpB 2"
FT                   /id="PRO_0000191086"
FT   DOMAIN          6..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          9..73
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..342
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          343..551
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          561..772
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          773..872
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          393..527
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         611..618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   872 AA;  98624 MW;  5C7558CB8943AE97 CRC64;
     MQPTNPNQFT EKAWEAIAHT PEIAKQHQQQ QIESEHLMKA LLEQDGLASG ILTKAGVNLQ
     KISDRTEQYI QRQPKVSGNS TSVYLGRSLD TLLDRAEAHR KDFQDEYISI EHLLLAYPKD
     DRFGKGLFQE FALDESKLKN IIKQVRGSQT VTDQNPEGKY QSLEKYGRDL TEAARKGQLD
     PVIGRDDEIR RTIQILSRRT KNNPVLIGEP GVGKTAIAEG LAQRIVAGDV PQSLKDRKLI
     SLDMGAMIAG AKFRGEFEER LKAVLKEVTE SGGNIVLFID EIHTVVGAGA TQGAMDAGNL
     LKPMLARGEL RCIGATTLDE YRKYIEKDAA LERRFQQVYV DQPSVEDTIS ILRGLKERYE
     VHHGVKISDS SLVAAATLSS RYISDRFLPD KAIDLVDEAA ARLKMEITSK PEELDEIDRK
     ILQLEMEKLS LQKESDAASR ERLERLEKEL ADLKEEQRTL NTQWQSEKDV INKLQSVKEE
     IDKVNLEIQQ AERNYDLNRA AELKYGNLTD LHRRLEATER ELSQTQGTGK SLLREEVTEA
     DIAEIISKWT GIPISKLVES EKEKLLHLED ELHHRVIGQD EAVTAVADAI QRSRAGLADP
     NRPTASFVFL GPTGVGKTEL AKALASYMFD TEDALVRIDM SEYMEKHAVS RLIGAPPGYV
     GYEEGGQLTE TIRRRPYAVI LFDEIEKAHP DVFNIFLQIL DDGRVTDAQG HTVDFKNTII
     IMTSNIGSQY ILDIAGDNSR YDEMRHRVME AMRNSFRPEF LNRIDEVIIF HSLDKKELRQ
     IVQLQVERLK ARLDDRKISL RLSDVALDFL AEVGYDPVFG ARPLKRAIQR ELETQIAKAI
     LRGEFNDGDT IFVDVQNERL SFSRLPVEVF SS