ID   CLPB_PROMP              Reviewed;         860 AA.
AC   Q7V2A3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=PMM0580;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
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; BX548174; CAE19039.1; -; Genomic_DNA.
DR   RefSeq; WP_011132214.1; NC_005072.1.
DR   AlphaFoldDB; Q7V2A3; -.
DR   SMR; Q7V2A3; -.
DR   STRING; 59919.PMM0580; -.
DR   PRIDE; Q7V2A3; -.
DR   EnsemblBacteria; CAE19039; CAE19039; PMM0580.
DR   KEGG; pmm:PMM0580; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_3; -.
DR   OMA; KRYITDH; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000001026; 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   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; 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; 1.
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   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; Repeat;
KW   Stress response.
FT   CHAIN           1..860
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191160"
FT   DOMAIN          5..145
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..145
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          157..338
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          339..548
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          558..769
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          770..860
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          389..523
FT                   /evidence="ECO:0000250"
FT   BINDING         204..211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         608..615
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   860 AA;  97364 MW;  57C75FFA3B960A1E CRC64;
     MKFVPSEFSN SAWDIFILSK EIAQNNFQQN IDSENILLAL IKQDLLTSKI LKKNCVNIRK
     IETKLTSLLD AKAKMKNKQK TLFIGETTEK VFLKANDLRV SFNDVVISTE HILYGLSYDE
     ICSELVLNTK KIPEFLELLN KMKSESTIND NFESSNETLD KFGIDLTKSA RDGILDPVIG
     RDEEIRRTIQ ILSRRTKNNP VLIGEPGVGK TAIVEGLAQR IVNGDVPSSL NNRQLISIDM
     GSLIAGAKYR GEFEERIKNV LKKVKSSEGK IILFIDEIHT VVGAGATGGS LDASNLLKPM
     LARGELRCIG ATTINEHKQN IEKDPALERR FQKIKINAPS VDDTISILRG LREKYEVHHS
     VRISDNALVA AASLSERYIN DRFLPDKAID LIDEAASRLN MIITSKPEEI DEIDRKVLQL
     EMENLSLQRE SDNFSLERLK RINNELHDLK IRQSELNHQW QKEKEEIDEI SNLKEEIEST
     QLKIEQAKRS FDLNKAAELE FGTLISLQKK LKIKSENLVD SFKSGEKNLL RQEVNFDDIA
     EVVSKWTSIP VNNLNQSEKE KLLKLELTLK EKIIGQNNAI CAVSDSIKRS RTGLNDPNRP
     IASFLFLGPT GVGKTELSKV IAKTIFDSNS SITRLDMSEY MEKHSVSKII GAPPGYLGFE
     SGGQLTEAVR KNPYSLILLD EIEKAHKDVL DVLLQVLDDG IITDGQGRTI SFKNSIIVLT
     SNLGSQSIND LSIRNEDKNE IKNIVNVELK KFFKPEFLNR LDEIIIFQNL ELNELKDIAK
     LQLKKLENRL IKKDLNFQIT DEAIDHLVKN SFDNSYGARP LKRIIQKEIE TKIANNILNN
     NYLNKKEVYI SIKDGCIFVN