ID   CLPB_LISMF              Reviewed;         866 AA.
AC   Q71XF9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=LMOf2365_2239;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT05006.1; -; Genomic_DNA.
DR   RefSeq; WP_003726239.1; NC_002973.6.
DR   AlphaFoldDB; Q71XF9; -.
DR   SMR; Q71XF9; -.
DR   PRIDE; Q71XF9; -.
DR   KEGG; lmf:LMOf2365_2239; -.
DR   HOGENOM; CLU_005070_4_0_9; -.
DR   OMA; GPEHILM; -.
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..866
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191136"
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..551
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          561..772
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          773..866
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         611..618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   866 AA;  97526 MW;  8A6130EB89180051 CRC64;
     MDLQKFTQQV QQTIADAQNL AIASEHQEID VAHVFKVLLT ESDFAKRVYD VAEVDIDALQ
     KTVEDALTKI PVVSGSGVNY GQAMSQALFQ LMRDAEKEQK QLDDDFVSTE HLILAVMDQK
     SNPITMNLKK QHKSKKQIQE AILKIRGGKK VTSQNAEENY EALTKYGRDL VAEVRSGKLD
     PVIGRDAEIR NVIRILSRKT KNNPVLIGEP GVGKTAIVEG LAQRIVRKDV PEGLKDKTII
     SLDIGSLIAG AKYRGEFEER LKAVLQEVKQ SDGQILLFID EIHTIVGAGK TDGAMDAGNM
     LKPMLARGEL HCIGATTLDE YRQYIEKDAA LERRFQKVLV PEPTVEDTVS ILRGLKERFE
     IHHGVNIHDN ALVAAASLSN RYITDRFLPD KAIDLVDEAC ATIRVEIDSM PSELDEVTRK
     VMQLEIEEAA LKEEKDPASE RRLEILQREL ADYKEEANQM KSKWESEKNE ISKIREVREQ
     IDHLRHELEE AENNYDLNKA AELRHGKIPA VEKELLELEA ENREKTAQED RILQEEVTEN
     EIAEIVGRWT GIPVTKLVEG EREKLLKLAD ELHQKVIGQD DAVQLVSDAV LRARAGIKDP
     KRPIGSFIFL GPTGVGKTEL AKALAFNMFD SEDHMIRIDM SEYMEKHSVS RLVGAPPGYV
     GYEEGGQLTE AVRRNPYSIV LLDEIEKAHP DVFNILLQVL DDGRITDSQG RLIDFKNTVI
     IMTSNIGSNL LLERTEEGEI SPELESDVMQ ILQSEFKPEF LNRVDDIILF KPLTLADIKG
     IVEKLVEELQ IRLADQEITI TISDNAKAFI AEEAYDPVYG ARPLKRYIVR HVETPLAREI
     VSGKIMPHSS VEIDLADKEF TFKVTE