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Database: UniProt
Entry: A0A075WU55_9BACT
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ID   A0A075WU55_9BACT        Unreviewed;       863 AA.
AC   A0A075WU55;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   08-NOV-2023, entry version 53.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=HL41_03560 {ECO:0000313|EMBL:AIH03928.1};
OS   Thermodesulfobacterium commune DSM 2178.
OC   Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC   Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC   Thermodesulfobacterium.
OX   NCBI_TaxID=289377 {ECO:0000313|EMBL:AIH03928.1, ECO:0000313|Proteomes:UP000028481};
RN   [1] {ECO:0000313|EMBL:AIH03928.1, ECO:0000313|Proteomes:UP000028481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2178 {ECO:0000313|EMBL:AIH03928.1,
RC   ECO:0000313|Proteomes:UP000028481};
RX   PubMed=25635017;
RA   Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA   Robb F.T., Ward N.L., Eisen J.A.;
RT   "Genome Sequence of a Sulfate-Reducing Thermophilic Bacterium,
RT   Thermodesulfobacterium commune DSM 2178T (Phylum Thermodesulfobacteria).";
RL   Genome Announc. 3:0-0(2015).
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; CP008796; AIH03928.1; -; Genomic_DNA.
DR   RefSeq; WP_038060385.1; NZ_JQLF01000005.1.
DR   AlphaFoldDB; A0A075WU55; -.
DR   STRING; 289377.HL41_03560; -.
DR   PaxDb; 289377-HL41_03560; -.
DR   KEGG; tcm:HL41_03560; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_0; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000028481; 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; IPR017729; ATPase_T6SS_ClpV1.
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   NCBIfam; TIGR03345; VI_ClpV1; 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:UP000028481};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          405..572
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   863 AA;  98276 MW;  0A107EF103B110AC CRC64;
     MKLDRYTFKA QEALQEAQKL AESKNNPQLE PEHLLLALVT QEGGIIPTIL DRLGVNSKII
     ASELEEILDK FPKLTQGAYQ LYLSLNLKQI LDKAEGLARE MRDEYVSTEH LFLAIIDSPT
     KAGEILRKRG VTFSNTKEVI NKIRKGQRIT DQNPEEKYQS LEKFGRDLTA LAKAGKLDPV
     IGRDEEIRRV MHILSRRTKN NPVLVGEPGV GKTAIVEGLA QRIVAGDVPE ILKNKRIIQL
     DLGSLIAGTK FRGEFEERLK AVLREVQASE GEIILFIDEI HTLVGAGAAE GAMDAANMLK
     PALARGELRC IGATTIDEYR KYIEKDPALE RRFQPVYVDE PSPEEAIAIL RGLKEKYEVH
     HGVKITDNAI VAAVMLSHRY ITDRFLPDKA IDLIDEAAAK LRIEIDSMPT EIDEIERKIK
     QLEIEKVALE KETDPKAKER LTKILEQLQD LRNKVEQLKE QWLKEKEIIQ KIRKLKERID
     QLKVEAQQAE RKGDLNRVAE IIYGIIPQLQ KELEEENRKL AEIQKEHKFL KEEVDAEDIA
     QIISKWTGIP VSRLLESERE KLLRIEEKLK ERVVGQDHAI KVIADALRRA RAGLKDPNRP
     IGSFMFIGPT GVGKTELAKA LAEFMFDTED AMIRIDMTEY MEKHSVSRLI GAPPGYVGYE
     EGGQLTEAVR RRPYSVILFD EIEKAHPDVF NILLQVLDDG RLTDGKGRTV DFRNTIIIMT
     SNVGSFYFQD LSISHTEIES KIHELLKATF KPEFLNRIDE IIIFNNLQRE HIIKIVDIQI
     KYLNERLAEK NMGLELTEKA KELIATYGYD PTFGARPLKR AIQRHIENPL ALKILDGTFV
     EGDKIIVDVN DFGEFVFTKQ PVH
//
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