ID   CLPB1_PARMW             Reviewed;         862 AA.
AC   Q7U637;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Chaperone protein ClpB 1;
GN   Name=clpB1; OrderedLocusNames=SYNW1503;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE08018.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX569693; CAE08018.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_042503620.1; NC_005070.1.
DR   AlphaFoldDB; Q7U637; -.
DR   SMR; Q7U637; -.
DR   STRING; 84588.SYNW1503; -.
DR   PRIDE; Q7U637; -.
DR   EnsemblBacteria; CAE08018; CAE08018; SYNW1503.
DR   KEGG; syw:SYNW1503; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_3; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000001422; 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; Repeat;
KW   Stress response.
FT   CHAIN           1..862
FT                   /note="Chaperone protein ClpB 1"
FT                   /id="PRO_0000191190"
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..550
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          560..771
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          772..862
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         610..617
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   862 AA;  95612 MW;  7CC86158A8898F25 CRC64;
     MQPTAEQFTE QAWAAIVAAQ QLAQASRHQQ LETEHLLLAL LRQNGLAGRI LSKTGVDVTT
     FEASVEGHLQ RLPSLGSAPD SVFLGRSLNK ALDRAEQRRD GFGDSFIAIE HLLLALAEDD
     RCGRQLLSQA GVTTNTLKEA ITAVRGNQTV TDQNPEATYE SLAKYGRDLT AAARDGQLDP
     VIGRDEEIRR TIQILSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVNGDVP QALQNRQLIT
     LDMGALIAGA KYRGEFEERL KAVLKEVTTS DGQIVLFIDE IHTVVGAGAS GGAMDASNLL
     KPMLARGELR CIGATTLDEH RQHIEKDPAL ERRFQQVLVD QPTVPDTISI LRGLKERYEV
     HHGVRIADSA LVAAAMLSSR YITDRFLPDK AIDLVDESAA RLKMEITSKP EQIDEIDRKI
     LQLEMEKLSL GRESDSASQE RLQRIERELA ELGEQQSSLN AQWQSEKGAI DQLSALKEEI
     ERVQLQVEQA KRNYDLNKAA ELEYGTLATL QRQLQEQEDL LEDEDGTDKT LLREEVTEDD
     IAEVIAKWTG IPVARLVQSE MEKLLQLEDD LHQRVIGQNQ AVTAVADAIQ RSRAGLSDPN
     RPIASFLFLG PTGVGKTELS KALANRLFDS DDAMVRIDMS EYMEKHTVSR LIGAPPGYVG
     YEAGGQLTEA VRRRPYAVIL FDEVEKAHPD VFNVMLQILD DGRVTDGQGR TVDFTNTVLI
     LTSNIGSQSI LELAGDPEQH TAMEQRVNEA LKAKFRPEFL NRLDDQIIFR SLEKEELRRI
     VSLQVERLRS RLEQRKLDLQ LSDIAADWLA TIGFDPVYGA RPLKRAIQRE LETPIAKAIL
     AGQLSEGQTV QVDAGDDKLS IS