ID   CLPB_GEOSL              Reviewed;         865 AA.
AC   Q74FF1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=GSU0658;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(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; AE017180; AAR33988.1; -; Genomic_DNA.
DR   RefSeq; NP_951715.1; NC_002939.5.
DR   RefSeq; WP_010941319.1; NC_002939.5.
DR   AlphaFoldDB; Q74FF1; -.
DR   SMR; Q74FF1; -.
DR   STRING; 243231.GSU0658; -.
DR   PRIDE; Q74FF1; -.
DR   EnsemblBacteria; AAR33988; AAR33988; GSU0658.
DR   KEGG; gsu:GSU0658; -.
DR   PATRIC; fig|243231.5.peg.654; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_7; -.
DR   InParanoid; Q74FF1; -.
DR   OMA; ERMKAVM; -.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; 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..865
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191124"
FT   DOMAIN          4..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          7..72
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..770
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          771..865
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          393..528
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   865 AA;  96456 MW;  5B7A53A30E2735CC CRC64;
     MIRPEKMTIK TQEALAGAQQ LAARQGNGSI EPEHLLVSLL EQEGGLIAPI IQKVGGAPAA
     LRSAADVLVK RLPQVSGATA QAYLSPALNR ILDAAQREAD TMKDEFVSTE HLLLGFFADR
     QCAAARALLD AGVSRDNVLA ALMEIRGGER VTDQNPEDTY QALAKYARDL TDLARQGKLD
     PVIGRDDEIR RVLQVLSRRT KNNPVLIGEP GVGKTAIVEG LAQRIVSGDV PETLKDKRLV
     ALDMGALIAG AKYRGEFEER LKAVIREVAK SEGKVILFID ELHTLVGAGA AEGAMDASNM
     LKPALARGEL HCIGATTLNE YRKYIEKDAA LERRFQQVYT GEPSVEDTIA ILRGLKEKYE
     NYHGIRIKDS AIIAAATLSD RYITDRFLPD KAIDLIDEAA SRLRIEIDSM PTEIDEVERR
     IIQLEIEKQA LLRESQDPHS LERLKKLADE LEELKAKSAE LKGHWQREKD IIGRVSSLRQ
     RLEEKREEAK KAEREGNLAR TAEIRYGEIP AIEKEIADRS AELEDIRKEG KMLPEEVDGE
     LVAEIVSRWT GIPVSRMMEG EADKLVHMED RLITRVVGQD EALVLVANAI RRARSGLSDP
     NRPIGSFLFL GPTGVGKTET AKALAEFLFN DDQAIVRIDM SEYQEKHTVA RLIGAPPGYV
     GYEEGGQLTE AVRRRPYSIV LFDEIEKAHP EVFNVLLQVL DDGRLTDGQG RTVDFRNTVI
     IMTSNLGSQW IQQYGSSDYA RMKAMVTETL KEGFKPEFLN RIDEIVIYHA LPLEQIKKIV
     DIQVECLKQR LADRRIVLEL SDKAREYLSR EGYDPAYGAR PLKRTIQRKI QDPLALALLE
     GKFQEGDTVR VDLSVSGEEL VITKK