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Database: UniProt
Entry: Q0KDX2_CUPNH
LinkDB: Q0KDX2_CUPNH
Original site: Q0KDX2_CUPNH 
ID   Q0KDX2_CUPNH            Unreviewed;       904 AA.
AC   Q0KDX2;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=ATP-dependent protease Clp, ATPase subunit {ECO:0000313|EMBL:CAJ91799.1};
GN   Name=clpC1 {ECO:0000313|EMBL:CAJ91799.1};
GN   OrderedLocusNames=H16_A0651 {ECO:0000313|EMBL:CAJ91799.1};
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ91799.1, ECO:0000313|Proteomes:UP000008210};
RN   [1] {ECO:0000313|EMBL:CAJ91799.1, ECO:0000313|Proteomes:UP000008210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   337 {ECO:0000313|Proteomes:UP000008210};
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
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   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675}.
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DR   EMBL; AM260479; CAJ91799.1; -; Genomic_DNA.
DR   RefSeq; WP_011614630.1; NZ_CP039287.1.
DR   AlphaFoldDB; Q0KDX2; -.
DR   STRING; 381666.H16_A0651; -.
DR   GeneID; 57642747; -.
DR   KEGG; reh:H16_A0651; -.
DR   PATRIC; fig|381666.6.peg.1020; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_1_0_4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000008210; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR017729; ATPase_T6SS_ClpV1.
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; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03345; VI_ClpV1; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 1.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:CAJ91799.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:CAJ91799.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008210};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          9..155
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          163..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   904 AA;  97454 MW;  BC06810B5B9B2C13 CRC64;
     MDISRQALFG RLNLTLFKAI ESATAFCKLR GNPYVELVHW LHQLLQAPDG DLQRMLRHAG
     ADLSVLEADL TRALAALPAG ATSISDFSFQ LESAIERAWV YATLAFSDDH VRGAYLLAAL
     LKTPELRRTV LGISSQFAKV RPDDLVEMAP ALIAQSPESR EAAYDGSGLA PATPGEASGA
     TAPASAGKPA LGRYCRDLTE EARAGRLDPV IGREHEIRTM TDILLRRRQN NPLLTGEAGV
     GKTAVIEGLA QAIAAGEVPP SLKDIRLLSL DVGALLAGAS MKGEFEARLK GVLEEAAKSP
     TPVILFVDEV HTLVGAGGQA GTGDAANLLK PALARGTLRT IGATTWSEYK RHIEKDPALT
     RRFQVLQVME PDEARAVAMV RGLVRTFEAH HQVLIRDEGV RAAVRLSHRF IPSRQLPDKA
     ISLLDTACAR VALSLHAPPA EVEHLRHELA AADAECALLA REAGFGRPDA ARIALARARR
     EQFEADLALA SARWDRVRGL ATDLVARRYA LVQSASDEST VAAPARRTLD ELEGHLHAAQ
     ADAPLVYTEV DERVVAAIVA DWTGIPVGRM VADEVATVMQ LPQTLGERVI GQGHALTQLG
     ERVTTARAQL TDPNKPVGVF LLAGPSGVGK TETALALADA LYGGEQNLIT INLSEFQEPH
     TVSTLKGAPP GYVGYGEGGV LTEAVRRRPY SVVLLDEVEK AHADIHEVFY QVFDKGYMED
     GEGRHIDFRN TILLLTSNAG SDLLANLCED PALMPEPAAL RDALMPELRK VFPAAFLGRL
     VVVPYLPLAA ENLGRIVRLH LDRVAVRMQH QHGIVLTYDD PVVEFIVARC PVGETGARQL
     IGFIEQVIQP QLARLWLLAL SEKRELAVIA IRVADSAPAG LAYHTEYRVG HDAVVPECPE
     AGSA
//
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