Overview
| Uniprot ID | A0A0P0WQ12 |
|---|
| Protein Name | ATP synthase subunit beta, mitochondrial |
|---|
| Gene Name | Os05g0553000 |
|---|
| Organism | Oryza sativa subsp. japonica |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 64 |
PPAPATGKATGGGKI |
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits
Protein Sequence
10
MATRRALSSL
20
VRAASRLRGA
30
SPAPRPRGPL
40
HRPSPSGYLF
50
NRAAAYATAA
60
AAKEAAPPAP
70
ATGKATGGGK
80
ITDEFTGAGA
90
VGQVCQVIGA
100
VVDVRFDEGL
110
PPILTALEVL
120
DHNIRLVLEV
130
AQHLGENMVR
140
TIAMDGTEGL
150
VRGQRVLNTG
160
SPITVPVGRA
170
TLGRIMNVIG
180
EPIDEKGDIT
190
TNHFLPIHRE
200
APAFVEQATE
210
QQILVTGIKV
220
VDLLAPYQRG
230
GKIGLFGGAG
240
VGKTVLIMEL
250
INNVAKAHGG
260
FSVFAGVGER
270
TREGNDLYRE
280
MIESGVIKLG
290
DKQSESKCAL
300
VYGQMNEPPG
310
ARARVGLTGL
320
TVAEHFRDAE
G
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0045259 |
proton-transporting ATP synthase complex |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0016887 |
ATP hydrolysis activity |
| Biological Process |
GO:0006754 |
ATP biosynthetic process |
| Biological Process |
GO:1902600 |
proton transmembrane transport |
Reference
[1] Meng X, Baine JM, Yan T, Wang S. Comprehensive Analysis of Lysine Lactylation in Rice (Oryza sativa) Grains.. J Agric Food Chem 69(29):8287-8297. 2021 Jul 28. PMID: 34264677.