ID   CLPB_LACLA              Reviewed;         867 AA.
AC   Q9CFF3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=LL1525; ORFNames=L166407;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK05623.1; -; Genomic_DNA.
DR   PIR; E86815; E86815.
DR   RefSeq; NP_267681.1; NC_002662.1.
DR   RefSeq; WP_003130040.1; NC_002662.1.
DR   AlphaFoldDB; Q9CFF3; -.
DR   SMR; Q9CFF3; -.
DR   STRING; 272623.L166407; -.
DR   PaxDb; Q9CFF3; -.
DR   PRIDE; Q9CFF3; -.
DR   EnsemblBacteria; AAK05623; AAK05623; L166407.
DR   KEGG; lla:L166407; -.
DR   PATRIC; fig|272623.7.peg.1636; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_9; -.
DR   OMA; GPEHILM; -.
DR   Proteomes; UP000002196; 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..867
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191131"
FT   DOMAIN          3..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          6..70
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          84..148
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          161..342
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          343..548
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          558..770
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          771..867
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          393..527
FT                   /evidence="ECO:0000250"
FT   BINDING         208..215
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   867 AA;  97335 MW;  83CC744C8B82E829 CRC64;
     MDIEKMTTTM QEALGSAQQI AQVRHHQVIE VPHLWRIFVQ PNSFGANFYK DLGIDLDDYT
     NLIEKEIDKI NSVEGSNITY GQNLSPDLFQ IFTEADKIAQ KMGDEYLSTE IILLALFELK
     QNPLTSYLVS HGLTKAKAQA AIEKLRGGDK VTSQNAEETY KALEKYGVDL VAQVKSGKQD
     PVIGRDEEIR DVIRVLSRKT KNNPVLIGEP GVGKTAIVEG LAQRIVRKDV PENLKDKTIF
     SLDMGALIAG AKYRGEFEER LKAVLNEVKK SDGQIILFID ELHTIVGAGK TEGSMDAGNL
     LKPMLARGEL HLIGATTLDE YRKYMETDKA LERRFQKVLV TEPTVEDTIS ILRGLKERFE
     IHHGVTIHDN ALVAAATLSN RYITDRFLPD KAIDLVDEAS ATIRVEMNSL PTELDQANRR
     LMQLEIEEAA LKKERDDASK KRLEIIRGEI AELREENNQL KAQWEAEKKE VGNISEKRNE
     LEHARHELEE AQNEGNLEKA AALRYGKIPE IEKELKAIEE KAKSDDLSLV QESVTEEQIT
     EVVGRMTGIP ITKLVEGERE KLLHLPETLH QRVVGQDEAV EAVSDAIIRA RAGIQDPNRP
     LGSFLFLGPT GVGKTELAKA LAENLFDSEE HMVRIDMSEY MEKHSVSRLV GAPPGYVGYD
     EGGQLTEAVR RNPYTIILLD EIEKAHPDVF NILLQVLDDG RLTDSKGVLV DFKNTVLIMT
     SNVGSQYLLD NVGENGEISE ETTENVMSQL RAHFKPEFLN RIDDTILFKP LALEDIKNII
     VKMTSQLSHR LEEMDVQLEL SEEVKVWIAE NAYEPAYGAR PLKRYLTKVI ENPLAKLIIG
     GKIPPKSKVI VTLVENKIDF DIQTIAE