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Database: UniProt
Entry: J9DFR7_9PROT
LinkDB: J9DFR7_9PROT
Original site: J9DFR7_9PROT 
ID   J9DFR7_9PROT            Unreviewed;       881 AA.
AC   J9DFR7;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=IMCC14465_16080 {ECO:0000313|EMBL:EJW20721.1};
OS   alpha proteobacterium IMCC14465.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; PS1 clade.
OX   NCBI_TaxID=1220535 {ECO:0000313|EMBL:EJW20721.1, ECO:0000313|Proteomes:UP000004836};
RN   [1] {ECO:0000313|EMBL:EJW20721.1, ECO:0000313|Proteomes:UP000004836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC14465 {ECO:0000313|EMBL:EJW20721.1,
RC   ECO:0000313|Proteomes:UP000004836};
RX   PubMed=23209213; DOI=10.1128/JB.01888-12;
RA   Yang S.J., Kang I., Cho J.C.;
RT   "Genome Sequence of Strain IMCC14465, Isolated from the East Sea, Belonging
RT   to the PS1 Clade of Alphaproteobacteria.";
RL   J. Bacteriol. 194:6952-6953(2012).
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.
CC       {ECO:0000256|ARBA:ARBA00025613}.
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|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJW20721.1}.
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DR   EMBL; ALYF01000006; EJW20721.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9DFR7; -.
DR   STRING; 1220535.IMCC14465_16080; -.
DR   PATRIC; fig|1220535.3.peg.1599; -.
DR   eggNOG; COG0542; Bacteria.
DR   Proteomes; UP000004836; Unassembled WGS sequence.
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:UP000004836};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          7..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          417..497
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   881 AA;  97248 MW;  F3498509A1611783 CRC64;
     MEQKMLPENL TDKLKGFVGS AQGLALREGH QRFEPIHILK IFMDDAEGLA SGLIQVAGAN
     PDKIRDNLGA QLGKMPKVSG SGSQLIMSPE TVKVFSNAEE LAQKRGDSFI SVELLLLAML
     KTDDADTSRL LKEAGLTTDA LEKAIASLRK GRQADSASAE QSYEALERYT RDLTDDARNG
     KLDPVIGRDE EIRRSMQVLS RRTKNNPVLI GEPGVGKTAI AEGLALRIVD GDVPESLKGK
     KLLSLDMGSL IAGAKYRGEF EERLKSVLQD VTASEGGIVL FIDEMHTLVG AGAGEGAMDA
     SNLLKPALAR GELHCIGATT LDEYRKHVEK DAALARRFQP VFVNEPHVDD TISILRGLKE
     KYELHHGVRI TDAALVAATT MSNRYINDRF LPDKAIDLMD EAASRLRMQV DSKPEALDEL
     DRRMIQLKIE REALKKETDK NSADRLVKLE VELSDLEEKV SALSARWEHE KSRLSDMQKL
     KEQLDAARIE LEQAQRQGAL ERASELSYGI IPELEKQLEV DDAGNADNAA AQNAPLMLEE
     AVTEEHVAQI VSRWTGVPVD KLMSGEKEKL LAMEDVLHHR VIGQEEAISS VSRAVRRARA
     GLQDPARPIG SFLFLGPTGV GKTELCKALA AFLFDDESAI CRIDMSEYME KHAVARLIGA
     PPGYVGYEEG GALSEAVRRR PYQIILFDEI EKAHPDIFNV LLQVLDDGRL TDGQGRTVDF
     SNTLIIMTSN LGASHLAALA DSETVDKVRQ EVQDEVHGFF RPEFINRLDE MILFERLKED
     QMGDIVDVQL ARLETILQSR DIHLELVDDA RAWLARTGYD PVFGARPLKR VIQKEVQDPL
     AEKILAGEVT DNSVVYVGVH KAENKSDSDT LSFSTTPPTA N
//
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