ID A0A1S3EQ79_DIPOR Unreviewed; 635 AA.
AC A0A1S3EQ79;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial {ECO:0000313|RefSeq:XP_012865622.1};
GN Name=Clpx {ECO:0000313|RefSeq:XP_012865622.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012865622.1};
RN [1] {ECO:0000313|RefSeq:XP_012865622.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012865622.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|PROSITE-
CC ProRule:PRU01250}.
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DR RefSeq; XP_012865622.1; XM_013010168.1.
DR AlphaFoldDB; A0A1S3EQ79; -.
DR STRING; 10020.ENSDORP00000016237; -.
DR GeneID; 105981133; -.
DR KEGG; dord:105981133; -.
DR CTD; 10845; -.
DR InParanoid; A0A1S3EQ79; -.
DR OMA; HRSDFTN; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0009841; C:mitochondrial endopeptidase Clp complex; IEA:Ensembl.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:Ensembl.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
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:0046034; P:ATP metabolic process; IEA:Ensembl.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:Ensembl.
DR CDD; cd19497; RecA-like_ClpX; 1.
DR Gene3D; 1.10.8.60; -; 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 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 SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 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,
KW ECO:0000313|RefSeq:XP_012865622.1};
KW Chaperone {ECO:0000256|PROSITE-ProRule:PRU01250};
KW Hydrolase {ECO:0000313|RefSeq:XP_012865622.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|RefSeq:XP_012865622.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01250}.
FT DOMAIN 95..148
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT REGION 70..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
SQ SEQUENCE 635 AA; 69408 MW; 49FFCD8B9951F13B CRC64;
MPSCGACTCG AAAAAARLLT TSFTSAPRGI SCSRIHIPVL GRLGTFETQI LRRAPLRTFS
ETPAYFAAKD GTNKDGSGDG NKKSVSEGGS KKSGSGNSGK GGNQLRCPKC GDLCTHVETF
VSSTRFVKCE KCHHFFVVLS EADSKKSIIK EPESAAEAVK LAFQQKPPPP PKKIYNYLDK
YVVGQSFAKK VLSVAVYNHY KRIYNNIPAN LRQQAEVEKQ TSLTPRELEI RRREDEYRFT
KLLQIAGISP HGNALGASMQ QQVNQQIPQE KRGGEVLDSS HDDIKLEKSN ILLLGPTGSG
KTLLAQTLAK CLDVPFAICD CTTLTQAGYV GEDIESVIAK LLQDANYNVE KAQQGIVFLD
EVDKIGSVPG IHQLRDVGGE GVQQGLLKLL EGTIVNVPEK NSRKLRGETV QVDTTNVLFV
ASGAFNGLDR IISRRKNEKY LGFGTPSNLG KGRRAAAAAD LANRSGESNT HQDIEEKDRL
LRHVEARDLI EFGMIPEFVG RLPVVVPLHS LDEKTLVQIL TEPRNAVIPQ YQALFSMDKC
ELNVTEDALK AIAKLALERK TGARGLRSIM EKLLLEPMFE VPNSDIVCVE VDKDVVEGKK
EPGYIRTPAK ESSEEEYDSG VEEDGWPRQA DAANS
//