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Database: UniProt
Entry: F1SJL5_PIG
LinkDB: F1SJL5_PIG
Original site: F1SJL5_PIG 
ID   F1SJL5_PIG              Unreviewed;       619 AA.
AC   F1SJL5; A0A4X1TJ64;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 2.
DT   24-JAN-2024, entry version 77.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial isoform X2 {ECO:0000313|EMBL:HDB78622.1};
DE   SubName: Full=Caseinolytic mitochondrial matrix peptidase chaperone subunit {ECO:0000313|Ensembl:ENSSSCP00000005302.2, ECO:0000313|Ensembl:ENSSSCP00005041118.1};
GN   Name=CLPX {ECO:0000313|Ensembl:ENSSSCP00000005302.2,
GN   ECO:0000313|VGNC:VGNC:86780};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000005302.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000005302.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000005302.2,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HDB78622.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000005302.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   EMBL; DQIR01223145; HDB78622.1; -; Transcribed_RNA.
DR   EMBL; DQIR01262373; HDC17851.1; -; Transcribed_RNA.
DR   EMBL; DQIR01310459; HDC65937.1; -; Transcribed_RNA.
DR   PaxDb; 9823-ENSSSCP00000005302; -.
DR   Ensembl; ENSSSCT00000005437.5; ENSSSCP00000005302.2; ENSSSCG00000004927.5.
DR   Ensembl; ENSSSCT00005066364.1; ENSSSCP00005041118.1; ENSSSCG00005041422.1.
DR   VGNC; VGNC:86780; CLPX.
DR   eggNOG; KOG0745; Eukaryota.
DR   GeneTree; ENSGT00390000017625; -.
DR   HOGENOM; CLU_014218_0_1_1; -.
DR   OMA; HRSDFTN; -.
DR   TreeFam; TF312884; -.
DR   Proteomes; UP000008227; Chromosome 1.
DR   Bgee; ENSSSCG00000004927; Expressed in testis and 46 other cell types or tissues.
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:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 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   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:HDB78622.1};
KW   Hydrolase {ECO:0000313|EMBL:HDB78622.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:HDB78622.1};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F1SJL5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
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          584..619
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        584..599
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   619 AA;  67421 MW;  4CFAC85C7276F039 CRC64;
     MSGCGACTCG ASAARLITSS LASAQRGISC GRIHIPVLGR LGTFETQLLR RVPFRTFTET
     PAYFASKDGI SKDGSGDGNK KSASEGSSKK SGSGNSGKGG NQLRCPKCGD LCTHVETFVS
     STRFVKCEKC HHFFVVLSEA DSKKSIIKEP ESAAEAVKLA FQQKPPPPPK KIYNYLDKYV
     VGQSFAKKVL SVAVYNHYKR IYNNIPANLR QQAEVEKQTS LTPRELLQIA GISPHGNALG
     ASMQQQVNQQ IPQEKRGGEV LDSSHDDIKL EKSNILLLGP TGSGKTLLAQ TLAKCLDVPF
     AICDCTTLTQ AGYVGEDIES VIAKLLQDAN YNVEKAQQGI VFLDEVDKIG SVPGIHQLRD
     VGGEGVQQGL LKLLEGTIVN VPEKNSRKLR GETVQVDTTN ILFVASGAFN GLDRIISRRK
     NEKYLGFGTP SNLGKGRRAA AAADLANRSG ESNTHQDIEE KDRLLRHVEA RDLIEFGMIP
     EFVGRLPVVV PLHSLDEKTL VQILTEPRNA VIPQYQALFS MDKCELNVTE DALKAIARLA
     LERKTGARGL RSIMEKLLLE PMFEVPNSDI VCVEVDKEVV EGKKEPGYIR APTKESSEEE
     YDSGVEEEGW PRQADAANS
//
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