UniProt Accession

 EFGM_MOUSE; Q8K0D5; Q921D6; Q924I0 

Genbank Protein ID

 AF315511; BC013093; BC031772 

Genbank Nucleotide ID

 AAK58878.1; AAH13093.1; AAH31772.1 

Protein Name

 Elongation factor G, mitochondrial 

Protein Synonyms/Alias

 EF-Gmt; Elongation factor G 1, mitochondrial; mEF-G 1; Elongation factor G1 

Gene Name

 Gfm1 

Gene Synonyms/Alias

 Efg; Efg1; Gfm 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
176	PFLTFINKLDRMGSN	acetylation	[1]
540	VPFDFTHKKQSGGAG	acetylation	[1, 2, 3]
541	PFDFTHKKQSGGAGQ	acetylation	[4]
541	PFDFTHKKQSGGAGQ	succinylation	[4]
588	QFVPAVEKGFLDACE	acetylation	[3]
710	LRSCTEGKGEYTMEY	acetylation	[3]

Reference

 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 

Functional Description

 Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A- site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis (By similarity). 

Sequence Annotation

 NP_BIND 54 61 GTP (By similarity).
 NP_BIND 121 125 GTP (By similarity).
 NP_BIND 175 178 GTP (By similarity).
 MOD_RES 176 176 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; Complete proteome; Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 751 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; ISS:UniProtKB.
 GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
 GO:0070125; P:mitochondrial translational elongation; ISS:UniProtKB. 

Interpro

 IPR000795; EF_GTP-bd_dom.
 IPR009022; EFG_III-V.
 IPR000640; EFG_V.
 IPR027417; P-loop_NTPase.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
 IPR005225; Small_GTP-bd_dom.
 IPR004540; Transl_elong_EFG/EF2.
 IPR005517; Transl_elong_EFG/EF2_IV.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 

Pfam

 PF00679; EFG_C
 PF03764; EFG_IV
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2 

SMART

 SM00838; EFG_C
 SM00889; EFG_IV 

PROSITE

 PS00301; EFACTOR_GTP 

PRINTS

 PR00315; ELONGATNFCT.