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Database: UniProt
Entry: F1N155_BOVIN
LinkDB: F1N155_BOVIN
Original site: F1N155_BOVIN 
ID   F1N155_BOVIN            Unreviewed;       633 AA.
AC   F1N155;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 2.
DT   24-JAN-2024, entry version 74.
DE   SubName: Full=Caseinolytic mitochondrial matrix peptidase chaperone subunit X {ECO:0000313|Ensembl:ENSBTAP00000011038.6};
GN   Name=CLPX {ECO:0000313|Ensembl:ENSBTAP00000011038.6,
GN   ECO:0000313|VGNC:VGNC:27462};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000011038.6, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000011038.6, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000011038.6,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000011038.6}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000011038.6};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   AlphaFoldDB; F1N155; -.
DR   Ensembl; ENSBTAT00000011038.6; ENSBTAP00000011038.6; ENSBTAG00000008386.6.
DR   VEuPathDB; HostDB:ENSBTAG00000008386; -.
DR   VGNC; VGNC:27462; CLPX.
DR   eggNOG; KOG0745; Eukaryota.
DR   GeneTree; ENSGT00390000017625; -.
DR   HOGENOM; CLU_014218_0_1_1; -.
DR   OrthoDB; 452393at2759; -.
DR   TreeFam; TF312884; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000008386; Expressed in semen and 109 other cell types or tissues.
DR   ExpressionAtlas; F1N155; baseline and differential.
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:Ensembl.
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:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          93..146
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   REGION          68..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..613
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   633 AA;  69314 MW;  7FA426C04488ABBB CRC64;
     MSGCGACTCG AAAARIFSSS LVSAQRGISC SRIHIPVLGR LGTFETQLLR RAPFRAFTET
     PAYFASRDGI SKDGSGDGNK KSASEGSSKK SGSGNSGKGG NQLRCPKCGD LCTHVETFVS
     STRFVKCEKC HHFFVVLSEA DSKKSIIKEP ESAAEAVKLA FQQKPPPPPK KIYNYLDKYV
     VGQSFAKKVL SVAVYNHYKR IYNNIPANLR QQAEVEKQTS LTPRELEIRR REDEYRFTKL
     LQIAGISPHG NALGASVQQQ VNQQIPQEKR GGEVLDSSHD DIKLEKSNIL LLGPTGSGKT
     LLAQTLAKCL DVPFAICDCT TLTQAGYVGE DIESVIAKLL QDANYNVEKA QQGIVFLDEV
     DKIGSVPGIH QLRDVGGEGV QQGLLKLLEG TIVNVPEKNS RKLRGETVQV DTTNILFVAS
     GAFNGLDRII SRRKNEKYLG FGTPSNLGKG RRAAAAADLA NRSGESNTHQ DIEEKDRLLR
     HVEARDLIEF GMIPEFVGRL PVVVPLHSLD EKTLVQILTE PRNAVIPQYQ ALFSMDKCEL
     NVTEDALKAI ARLALERKTG ARGLRSIMEK LLLEPMFEVP NSDIVCVEVD KEVVEGKKEP
     GYIRAPTKES SEEEYDSGVE EEGWPRQADA ANS
//
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