ID A8ZXC0_DESOH Unreviewed; 862 AA.
AC A8ZXC0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 110.
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 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 78, MITOCHONDRIAL; 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
//