GenomeNet

Database: UniProt
Entry: A0A4P6U4G6_9NOCA
LinkDB: A0A4P6U4G6_9NOCA
Original site: A0A4P6U4G6_9NOCA 
ID   A0A4P6U4G6_9NOCA        Unreviewed;       426 AA.
AC   A0A4P6U4G6;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
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:QBJ95065.1};
GN   ORFNames=ERC79_03110 {ECO:0000313|EMBL:QBJ95065.1};
OS   Rhodococcus sp. ABRD24.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=2507582 {ECO:0000313|EMBL:QBJ95065.1, ECO:0000313|Proteomes:UP000292013};
RN   [1] {ECO:0000313|EMBL:QBJ95065.1, ECO:0000313|Proteomes:UP000292013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABRD24 {ECO:0000313|EMBL:QBJ95065.1,
RC   ECO:0000313|Proteomes:UP000292013};
RA   Jin H.;
RT   "Complete genome sequence of Rhodococcus sp. ABRD24.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP035319; QBJ95065.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4P6U4G6; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000292013; 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:QBJ95065.1};
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:QBJ95065.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000292013};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT   DOMAIN          1..54
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   BINDING         13
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         16
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         38
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         122..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   426 AA;  46576 MW;  3491FF9ED1B2C16C CRC64;
     MARIGDGGDL LKCSFCGKSQ KQVKKLIAGP GVYICDECID LCNEIIEEEL AESSEVKLDE
     LPKPAEIRDF LENYVIGQDA AKRTLAVAVY NHYKRIQAGD RGRDARGETV ELSKSNILML
     GPTGCGKTYL AQTLAKMLNV PFAIADATAL TEAGYVGEDV ENILLKLIQA ADYDVKRAET
     GIIYIDEVDK IARKSENPSI TRDVSGEGVQ QALLKILEGT QASVPPQGGR KHPHQEFIQI
     DTTNVLFIVA GAFAGLEKIV SDRIGKRGIG FGAEVRSKAE IDTQDHFAEV MPEDLIKFGL
     IPEFIGRLPI VASVTNLDKE SLVKILSEPK NALVKQYTRL FDMDGVVLEF TADSLEAIAD
     QAIHRGTGAR GLRAIMEEVL LPVMYDIPSR DDVAKVVVSA ETVNDNVLPT IVPRKSDHDE
     RRDKSA
//
DBGET integrated database retrieval system