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Database: UniProt
Entry: A0A3E1RHD6_9BURK
LinkDB: A0A3E1RHD6_9BURK
Original site: A0A3E1RHD6_9BURK 
ID   A0A3E1RHD6_9BURK        Unreviewed;       866 AA.
AC   A0A3E1RHD6;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:RFO98764.1};
GN   ORFNames=DIC66_02485 {ECO:0000313|EMBL:RFO98764.1};
OS   Rhodoferax lacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=2184758 {ECO:0000313|EMBL:RFO98764.1, ECO:0000313|Proteomes:UP000260665};
RN   [1] {ECO:0000313|EMBL:RFO98764.1, ECO:0000313|Proteomes:UP000260665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC26218 {ECO:0000313|EMBL:RFO98764.1,
RC   ECO:0000313|Proteomes:UP000260665};
RA   Park M.;
RT   "Rhodoferax soyangensis sp.nov., isolated from an oligotrophic freshwater
RT   lake.";
RL   Submitted (MAY-2018) 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. 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|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:RFO98764.1}.
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DR   EMBL; QFZK01000001; RFO98764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E1RHD6; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000260665; 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:UP000260665};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          410..466
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   866 AA;  95378 MW;  0DCDF97198788BAD CRC64;
     MRTDKLTTKF QEALGDAQSL ALGNDNAYIE PAHVLAAMLR QEDGPKALLQ RAGVNVGGLL
     TAAEAAIKKL PQVQGHEQVQ VGRDMVSLLQ AAEKESIKRS DQFVSSDMFL LALCDNKGDA
     GNLVRASGMN RKSLESAIEA VSGGQRVDSA DAEDQRESLK KYCVDLTERA RMGKLDPVIG
     RDDEIRRAIQ VLQRRTKNNP VLIGEPGVGK TAIVEGLAQR IVAGEVPDSL KGKRVLSLDM
     ASLLAGAKFR GEFEERLKNV LKDLAKDEGQ TIVFIDELHT MVGAGKAEGA MDAGNMLKPA
     LARGELHCVG ATTLDEYRKY IEKDAALERR FQKILVGEPT VEATIAILRG LKERYEVHHG
     VQITDPAIVA AAELSNRYIT DRFLPDKAID LIDEAASKIK IELDSKPELM DKKDRRLIQL
     QIEREAVKRE KDEASQKRLE LINEEIQSLQ KEIADLDELW KAEKAQAQGS KTIMQEVEKV
     RFQIKELTDK GDFNKAGELQ YGKLPELEKR LKDAQSQEAG KAQSAKDGGR AQLLRTMVGA
     EEIAEVVSRA TGIPVAKMMQ GEKDKLLQME VKLHDRVVGQ DEAIAAVSNA IRRSRSGLSD
     PNRPTGSFLF LGPTGVGKTE LCKALAGFMF DSEDHLIRID MSEFMEKHSV ARLIGAPPGY
     VGYEEGGYLT EAVRRKPYCV VLLDEVEKAH PDVFNVLLQV LDDGRLTDGQ GRTVDFKNTV
     IVMTSNIGSH LIQSMVGQDT DDIKEAVTGE LKNHFRPEFL NRIDETVVFH ALDAQNIASI
     AKIQLQVLMA RLSKLDLTLD VSDAAVAELA KVGFDPLYGA RPLKRAIQQR IENPLSRLLL
     EGKFVPKSTI RVGVDPILAP GEFSFN
//
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