ID   CLPB_PROMM              Reviewed;         865 AA.
AC   Q7V8B1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=PMT_0449;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(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; BX548175; CAE20624.1; -; Genomic_DNA.
DR   RefSeq; WP_011129828.1; NC_005071.1.
DR   AlphaFoldDB; Q7V8B1; -.
DR   SMR; Q7V8B1; -.
DR   STRING; 74547.PMT_0449; -.
DR   EnsemblBacteria; CAE20624; CAE20624; PMT_0449.
DR   KEGG; pmt:PMT_0449; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_3; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000001423; 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_0000191159"
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..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          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         611..618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   865 AA;  95779 MW;  E52459560CF5C260 CRC64;
     MQPTADQFTE KGWAAIVLAQ QLAQQRKHQQ LETEHLLLSL LQQNALAGRI LEKAGVSIGN
     LQTAVEAHLQ EQPTMQAAPD SVYLGKGVND LLDQAEKHKQ AFGDSFISIE HLLLALAGDN
     RCGRKLLNQA GVDAGKLKVA IDAVRGNQKV TDQNPEGTYE SLEKYGRDLS AAAREGKLDP
     VIGRDDEIRR TIQILSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVNGDVP AALQNRQLIT
     LDMGALIAGA KYRGEFEERL KAVLKEVTAS EGQIVLFIDE IHTVVGAGAT GGAMDASNLL
     KPMLARGELR CIGATTLDEH RQHIEKDPAL ERRFQQVLVD QPTVQDTISI LRGLKERYEV
     HHGVRIADNA LVAAAVLSSR YIADRFLPDK AIDLMDESAA RLKMEITSKP EEIDEIDRKI
     VQLEMEKLSL GRESDSVSKE RLEKLERELA ELAEQQSALN AQWQQEKGAI DDLSSLKEEI
     ERVQLQVEQA KRSYDLNKAA ELEYGTLAGL QKQLSEKETA LAQDGEAGDK SLLREEVTED
     DIADVIAKWT GIPVAKLVQS EMEKLLGLEA ELHQRVIGQE QAVQAVADAI QRSRAGLSDP
     NRPIASFLFL GPTGVGKTEL SKALASQLFD SEAALVRIDM SEYMEKHSVS RLIGAPPGYV
     GYEAGGQLTE AVRRRPYAVI LFDEVEKAHQ DVFNVMLQIL DDGRVTDGQG RTVDFTNTVL
     ILTSNIGSQS ILDLGGDDSQ YREMERRVHD ALHAHFRPEF LNRLDETIIF HSLRREELRQ
     IVALQVNRLR ERLCDRKLGL EISDTAADWL ANAGYDPVYG ARPLKRAIQR ELETPIAKSI
     LAGLYGDSQI VHVDVDVDQE RLSFR