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Database: UniProt
Entry: A8ZXC0_DESOH
LinkDB: A8ZXC0_DESOH
Original site: A8ZXC0_DESOH 
ID   A8ZXC0_DESOH            Unreviewed;       862 AA.
AC   A8ZXC0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Dole_2696 {ECO:0000313|EMBL:ABW68499.1};
OS   Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3) (Desulfococcus
OS   oleovorans).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfosudaceae; Desulfosudis.
OX   NCBI_TaxID=96561 {ECO:0000313|EMBL:ABW68499.1, ECO:0000313|Proteomes:UP000008561};
RN   [1] {ECO:0000313|EMBL:ABW68499.1, ECO:0000313|Proteomes:UP000008561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6200 / JCM 39069 / Hxd3
RC   {ECO:0000313|Proteomes:UP000008561};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA   Richardson P.;
RT   "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL   Submitted (OCT-2007) 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; CP000859; ABW68499.1; -; Genomic_DNA.
DR   RefSeq; WP_012176110.1; NC_009943.1.
DR   AlphaFoldDB; A8ZXC0; -.
DR   STRING; 96561.Dole_2696; -.
DR   KEGG; dol:Dole_2696; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_7; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000008561; 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:UP000008561};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..534
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   862 AA;  96028 MW;  CC3A9CB0D517E771 CRC64;
     MRFDKLTIKA QELLQAAQSD AGARGHQQIE PEHLLFAMLE ENTGIVASML GKHGASVDAV
     RRDTAEALEA MPKISGAAAE VYISRRAKAV LDVAFAQAAS MKDEYVSVDH LFLALLDEKG
     GKAASILKQH GVTKDAMLKA LLDIRGNQRV TDQNPEEKYK ALEKYSRDLT ELARQGKLDP
     VIGRDEEIRR IVQVLSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVAGDVS EGLKNKRIVA
     LDMASLIAGA KYRGEFEDRL KAVLKEVERA EGSIILFIDE LHTLVGAGAS EGAMDASNML
     KPALARGSLR CVGATTLDEY RKYIEKDAAL ERRFQPVFTG EPDVTDTISI LRGLKEKYEV
     HHGVKIKDAA LVAAATLSDR YITDRFLPDK AIDLVDECAS KMRIEIDSMP AEIDEIHRKI
     VQSEIEKEAL KKESDKESRK RLGALEEELA RLKEDHAELK AHWDREKGMI QTIRGIKKEI
     EELGVAQQQA ERQGDFAKAA EIRYGKSVEL NKKLEATEKE LAAFQADKKM LKEEVDAEDI
     AEVVSRWTGI PVSKMMEGER EKLVHMEDRL ALRVVGQNEA VSAVSDAVRR SRSGLQDPNR
     PIGSFIFLGP TGVGKTELAK ALAEFLFDSE QVIRVDMSEY MEKHAVARLI GAPPGYVGYE
     EGGYLTESVR RRPYSVVLFD EIEKAHPDVF NILLQLLDDG RMTDGHGRTV DFKNTIVIMT
     SNVGSHLIQE MSRANEDPDQ VKEQITDVLR QNFKPEFLNR IDEIIVFHNL DRDQIAKIVE
     IQVQRLGKRT AERGVSIVLS DAAKRFIAEK GYDPVYGARP LKRMIQKHIE NPLAMEILKG
     NIPENSTISV DVEGDGIVFR QA
//
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