ID   CLPB_PROMA              Reviewed;         864 AA.
AC   Q7VBL0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=Pro_1082;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAQ00127.1; -; Genomic_DNA.
DR   RefSeq; NP_875474.1; NC_005042.1.
DR   RefSeq; WP_011125234.1; NC_005042.1.
DR   AlphaFoldDB; Q7VBL0; -.
DR   SMR; Q7VBL0; -.
DR   STRING; 167539.Pro_1082; -.
DR   EnsemblBacteria; AAQ00127; AAQ00127; Pro_1082.
DR   GeneID; 54200424; -.
DR   KEGG; pma:Pro_1082; -.
DR   PATRIC; fig|167539.5.peg.1132; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_3; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000001420; 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..864
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191158"
FT   DOMAIN          5..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          8..72
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          84..147
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          160..341
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          342..552
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          562..773
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          774..864
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          392..526
FT                   /evidence="ECO:0000250"
FT   BINDING         207..214
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   864 AA;  98056 MW;  C078DA2B7A28CAD0 CRC64;
     MDIKTDNFTE ESWSSILQAQ SNAKGFHHQY IETEHLLKSL IQENDLAKSI IKKCNGSIDQ
     IKMHLNDFIK NQPKLKERPE NLFIGKHLQK TINESDQIKQ SFDDDFISIE HLLIALSKDQ
     RCCNKILIHE KIDPEILLKS IAEIRGNQKV TDQNPESKYE SLKKYGRDLT SAAREGILDP
     VIGRDDEIRR TIQILSRRTK NNPVLIGEPG VGKTAIVEGL AQRIINGDVP SALQNRQLIA
     LDMGALIAGA KYRGEFEERL KAVLKEVTSS QGQIVLFIDE IHTVVGAGAT GGAMDASNLL
     KPMLARGELR CIGATTINEH RQHIEKDPAL ERRFQQVLIS EPSIEDTISI LRGLKEKYEV
     HHGVRISDSA LVAAAVLSNR YISERYLPDK AIDLIDESAS KLKMEITSKP EELDEIDRKI
     IQLQMEKLSL KRESNLASQE KLNAIDNGLN ELKSKQSSLN KQWQEEKESI NTLSFLKEEI
     EKVQLQIEQA KRDYDLNRAA ELEYGTLNSL QNKLKQKEDL IMVNNNNDQK SLLLREEVTE
     NDITEVIAKW TSIPLTKLLK SDIEKLLDLE DKLNSKVIGQ KQAVQAVADS IQRSRTGLSD
     PSRPMGSFLL LGPTGVGKTE LSKSLAKELF DSEKAMIRID MSEYMEKHSI SRLIGAPPGY
     VGYESGGQLS EAVRRNPYSV ILFDEVEKAN SDVLNIMLQI LDEGRLTDGK GKNINFKNTI
     IILTSNVGSE SIIEMTNKKN EYELIEEVVR NQLKNYFKPE FLNRLDEQII FKSLKKEDLK
     KIVKLQIDKV KARLKDKGLE IELNEKVIDW IADKGYNPIY GARPIKRIIQ TKLETKLAKM
     ILKSKSEERS HYQLDIIDDQ IVFN