ID A0A4R3VCV5_9BURK Unreviewed; 861 AA.
AC A0A4R3VCV5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=EV686_102170 {ECO:0000313|EMBL:TCV01458.1};
OS Paracandidimonas soli.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Paracandidimonas.
OX NCBI_TaxID=1917182 {ECO:0000313|EMBL:TCV01458.1, ECO:0000313|Proteomes:UP000294692};
RN [1] {ECO:0000313|EMBL:TCV01458.1, ECO:0000313|Proteomes:UP000294692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100048 {ECO:0000313|EMBL:TCV01458.1,
RC ECO:0000313|Proteomes:UP000294692};
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:TCV01458.1}.
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DR EMBL; SMBX01000002; TCV01458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R3VCV5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000294692; 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:TCV01458.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TCV01458.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000294692};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 95678 MW; 4946E954B9DD91EB CRC64;
MRFDKFTTRF QQAIAEAQSL AGRNDNPYIE PLHVLAALLS DADSGTGSLL ARAGAAVNKL
IPAVNAAIAA LPQVQGAEGS QQASRELQAA FVRTDKEAAK RGDSYIASEL FLLALLDDKG
EAGRLLREAG LQRKALEAAI EAVRGGGNVS DQEGDSNREA LAKYTTDLTE RARQGKLDPV
IGRDDEIRRA IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNDEVPE TLRGKKVLSL
DLAALLAGAK FRGEFEERLK AVLKELSQDD GKTIVFIDEL HTMVGAGKAE GAMDAGNMLK
PALSRGELHC IGATTLDEYR KYIEKDAALE RRFQKVLVDE PDVESTIAIL RGLQERYELH
HGVAITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAAAR IRMEIDSKPE VMDRLDRRII
QLKIEREAVR KESDEASQRR LKVIEDELEK LQREYNDYEE VWKAEKAAVQ GSQSIKEEIE
RTRAEMAELQ RKGQFDKLAE LQYGKLPELE GRLKAAEAGQ QSSERPKLLR TEVGAEEIAE
VVSRATGIPV SKMMQGERAK LLGMESALHQ RVVGQDEAVS LVADAVRRSR AGLSDPNRPY
GSFLFLGPTG VGKTELTKAL AGFLFDSDEH MIRIDMSEFM EKHSVARLIG APPGYVGYEE
GGYLTEAVRR KPYSVVLLDE VEKAHPDVFN VLLQVLDDGR LTDGQGRTVD FRNTVIVMTS
NLGSQHIQTM AGQPYEVVKE VVWEELKTSF RPEFLNRIDE VVVFHSLDEK HIESIARIQL
QRLGERLAQQ EMRLEVSDMA LTQLAKAGFD PVFGARPLKR AIQQQIENPV ARLILEGRFG
PNDVVPVDWR DGKFVFERTL Q
//