Overview
| Uniprot ID | A0A287ADU8 |
| Protein Name | ATP-dependent clpX-like chaperone, mitochondrial |
| Gene Name | CLPX |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 171 |
KPPPPPKKIYNYLDK |
Function
ATP-dependent chaperone that functions as an unfoldase. As part of the ClpXP protease complex, it recognizes specific protein substrates, unfolds them using energy derived from ATP hydrolysis, and then translocates them to the proteolytic subunit (CLPP) of the ClpXP complex for degradation. Thanks to its chaperone activity, it also functions in the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. This chaperone is also involved in the control of mtDNA nucleoid distribution, by regulating mitochondrial transcription factor A (TFAM) activity
Protein Sequence
10
MSGCGACTCG
20
ASAARLITSS
30
LASAQRGISC
40
GRIHIPVLGR
50
LGTFETQLLR
60
RVPFRTFTET
70
PAYFASKDGI
80
SKDGSGDGNK
90
KSASEGSSKK
100
SGSGNSGKGG
110
NQLRCPKCGD
120
LCTHVETFVS
130
STRFVKCEKC
140
HHFFVVLSEA
150
DSKKSIIKEP
160
ESAAEAVKLA
170
FQQKPPPPPK
180
KIYNYLDKYV
190
VGQSFAKKVL
200
SVAVYNHYKR
210
IYNNIPANLR
220
QQAEVEKQTS
230
LTPRELEIRR
240
REDEYRFTKL
250
LQIAGISPHG
260
NALGASMQQQ
270
VNQQIPQEKR
280
GGEVLDSSHD
290
DIKLEKSNIL
300
LLGPTGSGKT
310
LLAQTLAKCL
320
DVPFAICDCT
330
TLTQAGYVGE
340
DIESVIAKLL
350
QDANYNVEKA
360
QQGIVFLDEV
370
DKIGSVPGIH
380
QLRDVGGEGV
390
QQGLLKLLEG
400
TIVNVPEKNS
410
RKLRGETVQV
420
DTTNILFVAS
430
GAFNGLDRII
440
SRRKNEKYLG
450
FGTPSNLGKG
460
RRAAAAADLA
470
NRSGESNTHQ
480
DIEEKDRLLR
490
HVEARDLIEF
500
GMIPEFVGRL
510
PVVVPLHSLD
520
EKTLVQILTE
530
PRNAVIPQYQ
540
ALFSMDKCEL
550
NVTEDALKAI
560
ARLALERKTG
570
ARGLRSIMEK
580
LLLEPMFEVP
590
NSDIVCVEVD
600
KEVVEGKKEP
610
GYIRAPTKES
620
SEEEYDSGVE
630
EEGWPRQADA
ANS
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0009841 |
mitochondrial endopeptidase Clp complex |
| Cellular Component |
GO:0005759 |
mitochondrial matrix |
| Cellular Component |
GO:0042645 |
mitochondrial nucleoid |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0016887 |
ATP hydrolysis activity |
| Molecular Function |
GO:0004176 |
ATP-dependent peptidase activity |
| Molecular Function |
GO:0140662 |
ATP-dependent protein folding chaperone |
| Molecular Function |
GO:0046872 |
metal ion binding |
| Molecular Function |
GO:0016504 |
peptidase activator activity |
| Molecular Function |
GO:0051082 |
unfolded protein binding |
| Biological Process |
GO:0046034 |
ATP metabolic process |
| Biological Process |
GO:0051603 |
proteolysis involved in protein catabolic process |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.