CLPX_PONAB
ID CLPX_PONAB Reviewed; 633 AA.
AC Q5R7N3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial;
DE Flags: Precursor;
GN Name=CLPX;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease
CC complex. Hydrolyzes ATP. Targets specific substrates for degradation by
CC the Clp complex. Can perform chaperone functions in the absence of
CC CLPP. Enhances the DNA-binding activity of TFAM and is required for
CC maintaining a normal mitochondrial nucleoid structure. ATP-dependent
CC unfoldase that stimulates the incorporation of the pyridoxal phosphate
CC cofactor into 5-aminolevulinate synthase, thereby activating 5-
CC aminolevulinate (ALA) synthesis, the first step in heme biosynthesis.
CC Important for efficient erythropoiesis through up-regulation of heme
CC biosynthesis. {ECO:0000250|UniProtKB:O76031}.
CC -!- SUBUNIT: Homohexamer that forms a ring structure; this hexamerization
CC requires ATP binding. Component of the Clp complex formed by the
CC assembly of two CLPP heptameric rings with two CLPX hexameric rings,
CC giving rise to a symmetrical structure with two central CLPP rings
CC flanked by a CLPX ring at either end of the complex. Interacts with
CC TFAM. {ECO:0000250|UniProtKB:O76031}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion
CC matrix, mitochondrion nucleoid {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|PROSITE-
CC ProRule:PRU01250}.
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DR EMBL; CR860081; CAH92227.1; -; mRNA.
DR AlphaFoldDB; Q5R7N3; -.
DR SMR; Q5R7N3; -.
DR STRING; 9601.ENSPPYP00000007444; -.
DR PRIDE; Q5R7N3; -.
DR eggNOG; KOG0745; Eukaryota.
DR InParanoid; Q5R7N3; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0009368; C:endopeptidase Clp complex; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
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: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:0051603; P:proteolysis involved in protein catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; 1.
DR TIGRFAMs; TIGR00382; clpX; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Chaperone; Metal-binding; Mitochondrion;
KW Mitochondrion nucleoid; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 57..633
FT /note="ATP-dependent Clp protease ATP-binding subunit clpX-
FT like, mitochondrial"
FT /id="PRO_0000314945"
FT DOMAIN 93..146
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
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"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 294..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 437
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O76031"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76031"
SQ SEQUENCE 633 AA; 69194 MW; 5D0D2C32526746CE CRC64;
MPSCGACTCG AAAARLITSS LASAQRGISG GRIHMSVLGR LGTFEAQILR RAPLRSFTET
PAYFASKDGI SKDGSGDGNK KSASEGSSKK SGSGNSGKGG NQLRCPKCGD LCTHVETFVS
STRFVKCEKC HHFFVVLSEA DSKKSIIKEP ESAAEAVKLA FQQKPPPPPK KIYNYLDKYV
VGQSFAKKVL SVAVYNHYKR IYNNIPANLR QQAEVEKQTS LTPRELEIRR REDEYRFTKL
LQIAGISPHG NALGASMQQQ 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
