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
//