ID   CLPB_LACPL              Reviewed;         867 AA.
AC   Q88VX7; F9UPM7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=lp_1903;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
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; AL935263; CCC79166.1; -; Genomic_DNA.
DR   RefSeq; WP_011101584.1; NC_004567.2.
DR   RefSeq; YP_004889680.1; NC_004567.2.
DR   AlphaFoldDB; Q88VX7; -.
DR   SMR; Q88VX7; -.
DR   STRING; 220668.lp_1903; -.
DR   EnsemblBacteria; CCC79166; CCC79166; lp_1903.
DR   KEGG; lpl:lp_1903; -.
DR   PATRIC; fig|220668.9.peg.1603; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_9; -.
DR   OMA; GPEHILM; -.
DR   PhylomeDB; Q88VX7; -.
DR   BioCyc; LPLA220668:G1GW0-1628-MON; -.
DR   Proteomes; UP000000432; 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_0000191132"
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..547
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          557..769
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          770..867
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          393..526
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         607..614
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   867 AA;  96570 MW;  308B9816E0DFD15C CRC64;
     MNPEQFTESL QQALQQAQQI AQTRRHQEIG VPHLFKFLTQ PGELVRQIFS EAGADLDQLQ
     TELDRELDDI AVVSGGNVQY GGSMSSSLAT LMQAADAKRK ALGDDYLATD TLALALMDQT
     GDQLTKYLNQ QGITAGQVKN AVDRIRGGQR VTSRNQEDQY QALEKYGVDL VKQARQGNQD
     PVIGRDEEIL DVIRILSRKT KNNPVLIGEP GVGKTAIVEG LAQRIVRGDV PENLKDKTLF
     SLDMGSLIAG AKYRGEFEER LKAVLKEIKK SDGQIIMFID EIHNIVGAGK TEGSMDAGNL
     LKPMLARGEL HLIGATTLDE YRQYMEKDKA LERRFQKVLV AEPSVEDTIS ILRGLKERFE
     IHHGVRIHDN ALVAAAKLSD RYITDRYLPD KALDLVDEAS AEIRVEMNSN PTELDQVNRQ
     LMRLEVEEAA LKKETDDASV KRLADVQKEL ASAKEKQRTL SERWDSEKKS LQALSDKKSA
     LDKAKHDLEN AENNYDLEQA AKLQHGTIPK LEQELKAMEA NDHHEDWLVE ESVTPDQIAN
     VVSRMTGIPV AKLVAGEREK LLHLADHLHE RVVGQDAAVD AVSDAVLRSR AGLQDPNRPL
     GSFMFLGPTG VGKTELAKAL AENLFDADDH MVRIDMSEYM EKESVSRLVG AAPGYVGYEE
     GGQLTEAVRR NPYSIVLFDE IEKAHPDVFN ILLQVLDDGR LTDGQGRTVD FKNTILIMTS
     NLGSELLLAG VDDQGHLSAD THQQVMQLVQ SRFKPEFLNR IDDIIMFTPL QLGAIEEIVV
     KLIDRLSARL QDREITLKIS DEAKKWIAKQ GYEPAYGARP LRRFITNHVE TPLAKEIIAG
     RVAPKSTVAI NLMDDHLVFE NQSTQPA