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Entry: H9ZSM5_THETH
LinkDB: H9ZSM5_THETH
Original site: H9ZSM5_THETH 
ID   H9ZSM5_THETH            Unreviewed;       399 AA.
AC   H9ZSM5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 63.
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   ORFNames=TtJL18_1455 {ECO:0000313|EMBL:AFH39335.1};
OS   Thermus thermophilus JL-18.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=798128 {ECO:0000313|EMBL:AFH39335.1, ECO:0000313|Proteomes:UP000007388};
RN   [1] {ECO:0000313|EMBL:AFH39335.1, ECO:0000313|Proteomes:UP000007388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL-18 {ECO:0000313|EMBL:AFH39335.1,
RC   ECO:0000313|Proteomes:UP000007388};
RX   PubMed=23405355; DOI=10.1128/genomeA.00106-12;
RA   Murugapiran S.K., Huntemann M., Wei C.L., Han J., Detter J.C., Han C.S.,
RA   Erkkila T.H., Teshima H., Chen A., Kyrpides N., Mavrommatis K.,
RA   Markowitz V., Szeto E., Ivanova N., Pagani I., Lam J., McDonald A.I.,
RA   Dodsworth J.A., Pati A., Goodwin L., Peters L., Pitluck S., Woyke T.,
RA   Hedlund B.P.;
RT   "Whole Genome Sequencing of Thermus oshimai JL-2 and Thermus thermophilus
RT   JL-18, Incomplete Denitrifiers from the United States Great Basin.";
RL   Genome Announc. 1:E00106-E00112(2013).
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; CP003252; AFH39335.1; -; Genomic_DNA.
DR   RefSeq; WP_014629940.1; NC_017587.1.
DR   AlphaFoldDB; H9ZSM5; -.
DR   STRING; 798128.TtJL18_1455; -.
DR   KEGG; ttl:TtJL18_1455; -.
DR   PATRIC; fig|798128.4.peg.1414; -.
DR   HOGENOM; CLU_014218_8_2_0; -.
DR   Proteomes; UP000007388; 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: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   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   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};
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         8
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         11
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         109..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   399 AA;  44391 MW;  54BC5001210CF621 CRC64;
     MKRPRPHCSF CGLRPPETGR LLESPIEDVY ICEDCVERAQ EILAQEERRA PKGPSRLPRP
     QEIKAHLDQY VVGQEAAKRA LSVAVYNHYK RLLHPEAEIG KANILLIGPT GTGKTLLAET
     LARFLDVPFA IADATTLTEA GYVGEDVENV LLRLLQNADF DVERAEMGIV YIDEIDKIAR
     KSENPSLTRD VSGEGVQQAL LKIIEGTVAN VPPQGGRKHP HQEFIPVNTK NILFILGGAF
     EGLENIVKAR VGKTTIGFTG GRREREEPLE VIPEDLIKFG MIPEFVGRAP LIVQLHPLGE
     DDLVRILTEP KNALVKQYQE LFRMEGIELR FTQAALREVA RRALKRGTGA RGLRAILEKA
     MVDLMFEAPG SGVKEIVFDL PHLDHPLKAL EEARLRQAS
//
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