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Database: UniProt
Entry: B9M182_GEODF
LinkDB: B9M182_GEODF
Original site: B9M182_GEODF 
ID   B9M182_GEODF            Unreviewed;       866 AA.
AC   B9M182;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:ACM19152.1};
GN   OrderedLocusNames=Geob_0790 {ECO:0000313|EMBL:ACM19152.1};
OS   Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS   daltonii).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM19152.1, ECO:0000313|Proteomes:UP000007721};
RN   [1] {ECO:0000313|EMBL:ACM19152.1, ECO:0000313|Proteomes:UP000007721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC   {ECO:0000313|Proteomes:UP000007721};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kostka J., Richardson P.;
RT   "Complete sequence of Geobacter sp. FRC-32.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP001390; ACM19152.1; -; Genomic_DNA.
DR   RefSeq; WP_012645881.1; NC_011979.1.
DR   AlphaFoldDB; B9M182; -.
DR   STRING; 316067.Geob_0790; -.
DR   KEGG; geo:Geob_0790; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_7; -.
DR   OMA; ERMKAVM; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000007721; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
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; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007721};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          4..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          414..494
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   866 AA;  96499 MW;  3BE880FCFF32706F CRC64;
     MIRPEKMTIK TQEALSQAQE AAAQRGNSAI EPEHLLSAML GQEGGLTGSI LQKMGVTPNL
     VNERLAEALR KLPRASGATM QVFLSPTLNH VLDAAQKEAD TMKDAFVSTE HLLLALVGEK
     GSIIAGILRE SGVTREGILA ALKDIRGDEK ITDQAAEDKY QALTKYARDL TDLARRGKLD
     PVIGRDDEIR RVIQVLSRRT KNNPVLIGEP GVGKTAIVEG LAQRIISGDV PETLRDKKLV
     ALDMGALIAG AKYRGEFEDR LKAVIKEVEK AEGKIILFID ELHTLVGAGA AEGAMDASNM
     LKPALARGEL HCIGATTLNE YRKHIEKDAA LERRFQQVYA GEPSVEDTIA ILRGLKERYE
     NYHSVRIKDS AIIAAATLSD RYITDRFLPD KAIDLIDEAA SRLRIEIDSM PTEIDEVERK
     VIQLEIEKQA LLREQDPHAK ERLRKISDEL EELRSSSATL KSQWQQEKSL LTSISDLKKQ
     LEEKKEQAKK SEREGDLALT AKLRYGEIPA IEKDIADKSN ELLQKQKEGK MLPEEVDGDM
     VAEIVAKWTG IPVNRMLETE SEKLVRMEER LKGRVVGQDE ALELVANAVR RSRSGLSDPN
     RPIGSFIFLG PTGVGKTETA RALAEFLFDD DQAIVRIDMS EYQERHTVAR LIGAPPGYVG
     YEEGGQLTEA IRRRPYSIVL FDEIEKAHSD VFNILLQVLD DGRLTDGQGR TVDFRNTVII
     MTSNLGSQFI QQYASGDYAK MRTMVMGTLR ENFKPEFLNR IDEIIIYHSL PLEQIKHIVS
     LQIKGLQKRL AERNLGLEIT GRASEYLAKE GYDPAYGARP LKRTLQKKVQ DPLALMLLQG
     KFQEGDTVVV DVAMDGDSLV IKKREP
//
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