ID   CLPB2_PARMW             Reviewed;         900 AA.
AC   Q7U3T3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Chaperone protein ClpB 2;
GN   Name=clpB2; OrderedLocusNames=SYNW2346;
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}.
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DR   EMBL; BX569695; CAE08861.1; -; Genomic_DNA.
DR   RefSeq; WP_011129199.1; NC_005070.1.
DR   AlphaFoldDB; Q7U3T3; -.
DR   SMR; Q7U3T3; -.
DR   STRING; 84588.SYNW2346; -.
DR   PRIDE; Q7U3T3; -.
DR   EnsemblBacteria; CAE08861; CAE08861; SYNW2346.
DR   KEGG; syw:SYNW2346; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_3; -.
DR   OMA; RYISDRC; -.
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   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; 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   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..900
FT                   /note="Chaperone protein ClpB 2"
FT                   /id="PRO_0000191191"
FT   DOMAIN          15..154
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          18..81
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          91..154
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          151..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..376
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          377..581
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          591..803
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          804..900
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          427..557
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        153..183
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         244..251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         641..648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   900 AA;  99782 MW;  F7CB9A1FE65C87C9 CRC64;
     MTGTPASRGS LTHEPDRFSD PAWELLLAGQ DMARRWRHDQ LDVEHLIQVL FSDSSFRRWV
     EPLPLRSDDL LDRLEDVLAD QPPARGDQLF IGEDLEQLLE TADQVRGRWG DRSIDVPQLI
     VAVGADPRIG AELFAAQGLA VDRLESLLRQ PSVSPAPAPP PVPTAASAPA PTPRSAPAPR
     VMAPEPEPMV ELEREPSALE AYGRDLTEEA EAGSLDPVIG RDSEIRNLIK VLSRRSKNNP
     VLIGEPGVGK TAIAELLAQR IVAGEVPDSL QGLRLIALDL GALIAGAKFR GQFEERLRSV
     LEEVSRSDSG VVLFIDELHT VVGSDRSSTD AGSLLKPALA RGDLRCIGAT TPEEYRRTVE
     KDPALNRRFQ QVLIREPDLE LSLEILRGLR ERYELHHGVT ITDEAIQTAN RLADRYISDR
     CLPDKAIDLI DEAAAQLKIE VTSKPQVVEE AEADLRRVEL ALLAAEEAPE EERIQLQRQR
     LEVSSRLDDL RRRWQEERTQ LEELGQLLQQ DEDLRHAIAE AEREGALEEA ARLQYDQLHT
     VQQRREALEA SQAEAQSAGT ALLREQVEAG DIADLVARWT GIPVQRLLAG ERRKLLALES
     HLSERVIGQV EAVAAVAAAI RRARAGMKDP RRPVGSFLFL GPTGVGKTEL AKALATSLFD
     EEEALVRLDM SEFMERNASA RLIGAPPGYV GYEEGGQLTE AVRRRPYAVL LLDEVEKAHP
     DVFNLLLQVL DDGRLTDSQG LTVDFRHTVV VMTSNLASPV ILEHARSGSS DDAQLQQQVD
     AALSSQFRPE FLNRIDEVIR FRPLKVKDLV RIVRLQLADL STLMAEQGLS LEVDDAVADS
     LARQGHEPEY GARPLRRVLR RQLENPLATQ LLEERFRSAH GIRVRCGTDD GASLEFEPLE