Overview
| Uniprot ID | F1SJL5 |
| 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
LTPRELLQIA
240
GISPHGNALG
250
ASMQQQVNQQ
260
IPQEKRGGEV
270
LDSSHDDIKL
280
EKSNILLLGP
290
TGSGKTLLAQ
300
TLAKCLDVPF
310
AICDCTTLTQ
320
AGYVGEDIES
330
VIAKLLQDAN
340
YNVEKAQQGI
350
VFLDEVDKIG
360
SVPGIHQLRD
370
VGGEGVQQGL
380
LKLLEGTIVN
390
VPEKNSRKLR
400
GETVQVDTTN
410
ILFVASGAFN
420
GLDRIISRRK
430
NEKYLGFGTP
440
SNLGKGRRAA
450
AAADLANRSG
460
ESNTHQDIEE
470
KDRLLRHVEA
480
RDLIEFGMIP
490
EFVGRLPVVV
500
PLHSLDEKTL
510
VQILTEPRNA
520
VIPQYQALFS
530
MDKCELNVTE
540
DALKAIARLA
550
LERKTGARGL
560
RSIMEKLLLE
570
PMFEVPNSDI
580
VCVEVDKEVV
590
EGKKEPGYIR
600
APTKESSEEE
610
YDSGVEEEGW
PRQADAANS
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0042645 |
mitochondrial nucleoid |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0016887 |
ATP hydrolysis activity |
| Molecular Function |
GO:0140662 |
ATP-dependent protein folding chaperone |
| Molecular Function |
GO:0046872 |
metal ion binding |
| Molecular Function |
GO:0008233 |
peptidase activity |
| Molecular Function |
GO:0051082 |
unfolded protein binding |
| Biological Process |
GO:0006508 |
proteolysis |
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.