CPLM-001815

Genbank Nucleotide ID

ATP synthase subunit beta, mitochondrial

Protein Synonyms/Alias

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Position	Peptide	Type	References
108	EGLVRGEKVLDTGGP	acetylation	[1]
143	IDERGPIKSKLRKPI	acetylation	[1]
196	FGGAGVGKTVFIQEL	methylation	[2]
235	NDLYREMKETGVINL	acetylation	[1]
334	ERITTTKKGSVTSVQ	methylation	[3]
434	DELSEQDKLTVERAR	ubiquitination	[4]
475	KDTVASFKAVLEGKY	acetylation	[1]

[1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
[2] Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications.
Pang CN, Gasteiger E, Wilkins MR.
BMC Genomics. 2010 Feb 5;11:92. [PMID: 20137074]
[3] High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans.
Cao XJ, Dai J, Xu H, Nie S, Chang X, Hu BY, Sheng QH, Wang LS, Ning ZB, Li YX, Guo XK, Zhao GP, Zeng R.
Cell Res. 2010 Feb;20(2):197-210. [PMID: 19918266]
[4] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]

Functional Description

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.

NP_BIND 190 197 ATP (By similarity).
MOD_RES 112 112 Phosphothreonine.
MOD_RES 237 237 Phosphothreonine.
MOD_RES 373 373 Phosphoserine.

3D-structure; ATP synthesis; ATP-binding; CF(1); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Hydrolase; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0016021; C:integral to membrane; ISM:SGD.
GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IDA:SGD.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:SGD.
GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO:0015986; P:ATP synthesis coupled proton transport; IDA:SGD.

IPR003593; AAA+_ATPase.
IPR020003; ATPase_a/bsu_AS.
IPR004100; ATPase_a/bsu_N.
IPR005722; ATPase_F1-cplx_bsu.
IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034; ATPase_F1_bsu/V1_C.
IPR027417; P-loop_NTPase.

PF00006; ATP-synt_ab
PF00306; ATP-synt_ab_C
PF02874; ATP-synt_ab_N

PS00152; ATPASE_ALPHA_BETA