GenomeNet

Database: UniProt
Entry: A0A4R6Y1T7_9BURK
LinkDB: A0A4R6Y1T7_9BURK
Original site: A0A4R6Y1T7_9BURK 
ID   A0A4R6Y1T7_9BURK        Unreviewed;       861 AA.
AC   A0A4R6Y1T7;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   13-SEP-2023, 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   ORFNames=DFR44_12124 {ECO:0000313|EMBL:TDR30408.1};
OS   Hydromonas duriensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Hydromonas.
OX   NCBI_TaxID=1527608 {ECO:0000313|EMBL:TDR30408.1, ECO:0000313|Proteomes:UP000294480};
RN   [1] {ECO:0000313|EMBL:TDR30408.1, ECO:0000313|Proteomes:UP000294480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 102852 {ECO:0000313|EMBL:TDR30408.1,
RC   ECO:0000313|Proteomes:UP000294480};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) 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:TDR30408.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; SNZE01000021; TDR30408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R6Y1T7; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000294480; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:TDR30408.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TDR30408.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000294480};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          414..494
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   861 AA;  95197 MW;  F9E51A332FEB60B5 CRC64;
     MNFEQFTSSF QTALQNAQSL AQEQGQSSID VAHVLAAMMA DVDGGLPALL RYTGVDLARV
     KALINQAVDD LPKVATHTSA PMLSSELVGL LQRAEKHAKQ YGDSYVASEM CLVALLDSDS
     RSPLKKQFNA MGLNEKTLMA AIESIRKGKN VDNPNAEGQR EALKKYTLDL TERARSGKLD
     PVIGRDDEIR RTIQILQRRS KNNPVLIGEP GVGKTAIVEG LAQRIVNGEV PDSLKDKRIL
     VLDMAALLAG AKYRGDFEER LKAVLNEVEQ DAGQTIMFID EIHTMVGAGK AEGSIDAGNM
     LKPALARGDL HCIGATTLNE YRGSLEKDAA LERRFQKVLV EEPSVESTIA ILRGLQEKYE
     VHHGVDITDP AIVAAATLSH RYITDRFLPD KAIDLIDEAA ARIKIEIDSK PELLDKLERR
     LIQLKIEREA LIRETDEASR ERLDLLEQEM KALEKELADL DEEWRREKAQ AQGSAQIKEK
     IDALRGDMVE LQRQGKLDKV AEIQYGQLPE LERQLKETEH AEKEDVKAKP RLLKTQVGVE
     EIAEVVSRST GIPVSKMLQG EREKLLSIAT HLHERVVGQN EAVDSVADVI MRSRAGLADP
     NKPYGSFLFL GPTGVGKTEL CKALAQFLFD SEDHLIRIDM SEYMEKHSVA RLIGAPPGYV
     GYESGGYLTE QVRRKPYSVI LFDEVEKAHP DVFNVLLQAL DDGRMTDGQG RTIDFKNTVM
     VMTSNLGSQE ISRLSGSSSD VIQTAVMNEV KQYFRPEFIN RIDEVVVFHH LTAANIQGIA
     KIQLQRLAAR LLEQDLTLNV TPAAVAAIAE AGFDAAYGAR PLKRAISQNI ENPLAREILA
     GHYLPKSVVT VDYGADGFVF V
//
DBGET integrated database retrieval system