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}.
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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
//