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Database: UniProt
Entry: A0A369CEA9_9GAMM
LinkDB: A0A369CEA9_9GAMM
Original site: A0A369CEA9_9GAMM 
ID   A0A369CEA9_9GAMM        Unreviewed;       430 AA.
AC   A0A369CEA9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:RCX32033.1};
GN   ORFNames=DFQ59_102383 {ECO:0000313|EMBL:RCX32033.1};
OS   Thioalbus denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalbus.
OX   NCBI_TaxID=547122 {ECO:0000313|EMBL:RCX32033.1, ECO:0000313|Proteomes:UP000252707};
RN   [1] {ECO:0000313|EMBL:RCX32033.1, ECO:0000313|Proteomes:UP000252707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26407 {ECO:0000313|EMBL:RCX32033.1,
RC   ECO:0000313|Proteomes:UP000252707};
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 (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01250}.
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:RCX32033.1}.
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DR   EMBL; QPJY01000002; RCX32033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369CEA9; -.
DR   OrthoDB; 6378724at2; -.
DR   Proteomes; UP000252707; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   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; 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:0000313|EMBL:RCX32033.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW   ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:RCX32033.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:RCX32033.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252707};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01250}.
FT   DOMAIN          1..49
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|PROSITE-ProRule:PRU01250"
FT   BINDING         11
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
SQ   SEQUENCE   430 AA;  46249 MW;  4D2BD03F3FA38F0B CRC64;
     MAEHPMKCSF CGTRHTPETP LIAGLEGHIC EDCVQLAATV VGSWGRRRRS DETLAPPPVP
     REIKRLLDAH VIGQDTAKEI LAVAVYNHYK RLAGMEGTRP ARIAAVEESP VVPEKSNILL
     LGPSGTGKTL LASTLARIVG VPFAIADATT LTQAGYVGDD VETLLIRLLD QADGDPRRAR
     NGIIYIDEID KLARAGDSAL GVRDVSGEGV QQALLKLVEG SEVSIPARGR RKEGAETVTL
     DTRNILFIAG GAFSGLERVV GERTAARGSG IGFHAPLTNS TEQRPGGDPL AEVVPEDLRR
     FGLIPEFIGR FPIIAPLHEL DERLLTRILT EPHNALVRQY QALFRYDDTE LEFTEEALMA
     IAHAALERGT GARGLRSVME RLLQRTMFEL PSMAGVRRCV VDRDAAGDIG VVPLFGTVPA
     GAEFAAEGAG
//
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