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Database: UniProt
Entry: D3DHC6_HYDTT
LinkDB: D3DHC6_HYDTT
Original site: D3DHC6_HYDTT 
ID   D3DHC6_HYDTT            Unreviewed;       411 AA.
AC   D3DHC6;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175};
GN   Name=clpX {ECO:0000256|HAMAP-Rule:MF_00175,
GN   ECO:0000313|EMBL:BAI69228.1};
GN   OrderedLocusNames=HTH_0768 {ECO:0000313|EMBL:BAI69228.1};
OS   Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC   Hydrogenobacter.
OX   NCBI_TaxID=608538 {ECO:0000313|EMBL:BAI69228.1, ECO:0000313|Proteomes:UP000002574};
RN   [1] {ECO:0000313|EMBL:BAI69228.1, ECO:0000313|Proteomes:UP000002574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6534 / IAM 12695 / TK-6 [Tokyo]
RC   {ECO:0000313|Proteomes:UP000002574};
RX   PubMed=20348262; DOI=10.1128/JB.00158-10;
RA   Arai H., Kanbe H., Ishii M., Igarashi Y.;
RT   "Complete genome sequence of the thermophilic, obligately
RT   chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter
RT   thermophilus TK-6.";
RL   J. Bacteriol. 192:2651-2652(2010).
CC   -!- FUNCTION: ATP-dependent specificity component of the Clp protease. It
CC       directs the protease to specific substrates. Can perform chaperone
CC       functions in the absence of ClpP. {ECO:0000256|HAMAP-Rule:MF_00175}.
CC   -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring
CC       that, in the presence of ATP, binds to fourteen ClpP subunits assembled
CC       into a disk-like structure with a central cavity, resembling the
CC       structure of eukaryotic proteasomes. {ECO:0000256|HAMAP-Rule:MF_00175}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|HAMAP-
CC       Rule:MF_00175, ECO:0000256|PROSITE-ProRule:PRU01250}.
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DR   EMBL; AP011112; BAI69228.1; -; Genomic_DNA.
DR   RefSeq; WP_012963409.1; NC_017161.1.
DR   AlphaFoldDB; D3DHC6; -.
DR   STRING; 608538.HTH_0768; -.
DR   KEGG; hth:HTH_0768; -.
DR   PATRIC; fig|608538.5.peg.779; -.
DR   eggNOG; COG1219; Bacteria.
DR   OMA; HYKRVQA; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000002574; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19497; RecA-like_ClpX; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 6.20.220.10; ClpX chaperone, C4-type zinc finger domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00175; ClpX; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR046425; ClpX_bact.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   InterPro; IPR038366; Znf_CppX_C4_sf.
DR   NCBIfam; TIGR00382; clpX; 1.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   Pfam; PF06689; zf-C4_ClpX; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SMART; SM00994; zf-C4_ClpX; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51902; CLPX_ZB; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00175};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175};
KW   Hydrolase {ECO:0000313|EMBL:BAI69228.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00175};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00175}; Protease {ECO:0000313|EMBL:BAI69228.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002574};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT   DOMAIN          1..51
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         32
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         117..124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   411 AA;  45891 MW;  065A639C4C42E1E2 CRC64;
     MKTYAKNRCS FCGRSQDEVL VLIAGPNDTF ICDRCVEACN SVIKEQKKQH TYHGLGSIPK
     PEKIKSFLDE YVVGQERAKR ILSVAVYNHY KRVKAKEMGL GFDDVEVEKS NILLIGPTGS
     GKTLLAKTLA KLLNVPFAIA DATSLTEAGY VGEDVENVLT RLLQNCGYDV KLAQMGIVYI
     DEIDKIAKKS GINPSITRDV SGEGVQQALL KIMEGTVANV PPQGGRKHPH QEFIQVDTTD
     ILFICGGAFV GLEDIIKRRL GKSTIGFESQ VKGAFKEMNV LELVEPDDLI HFGLIPEFIG
     RLPVIAVLDE LTEEDLVRIL TEPKNSLVKQ YKKLFEMDNV DLEFTQEALI EIARESIKRK
     TGARGLRAIM EEIMTDVMFE IPSMKGVKKV IIDEEVVRNR IKPKYVYKEA V
//
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