P02992 (EFTU_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor Tu, mitochondrial

Alternative name(s):
tufM

Gene names

Name:	TUF1
Synonyms:	TUFM
Ordered Locus Names:	YOR187W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	G-protein that, in its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled before binding another molecule of aminoacyl-tRNA. Required for mitochondrial protein biosynthesis and maintenance of mitochondrial DNA. Ref.4
Pathway	Protein biosynthesis; polypeptide chain elongation.
Subcellular location	Mitochondrion Ref.6 Ref.8.
Post-translational modification	The precursor is processed in two steps involving mitochondrial intermediate peptidase (MIP) and mitochondrial processing peptidase (MPP).
Miscellaneous	Present with 58527 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial translation Inferred from genetic interaction PubMed 15695360PubMed 16777356. Source: SGD
Cellular_component	mitochondrial matrix Inferred from sequence or structural similarity Ref.1. Source: SGD
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from direct assay PubMed 3301847. Source: SGD translation elongation factor activity Inferred from direct assay PubMed 3301847. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 38	38	Mitochondrion Probable
	Chain	39 – 437	399	Elongation factor Tu, mitochondrial		PRO_0000007465
Regions
	Nucleotide binding	55 – 62	8	GTP By similarity
	Nucleotide binding	117 – 121	5	GTP By similarity
	Nucleotide binding	172 – 175	4	GTP By similarity
Amino acid modifications
	Modified residue	100	1	Phosphoserine Ref.9
	Modified residue	101	1	Phosphothreonine Ref.9
	Modified residue	258	1	Phosphoserine Ref.10
	Modified residue	296	1	Phosphothreonine Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P02992 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 26F4DFE805D1A93B	FASTA	437	47,972
	10 20 30 40 50 60 MSALLPRLLT RTAFKASGKL LRLSSVISRT FSQTTTSYAA AFDRSKPHVN IGTIGHVDHG 70 80 90 100 110 120 KTTLTAAITK TLAAKGGANF LDYAAIDKAP EERARGITIS TAHVEYETAK RHYSHVDCPG 130 140 150 160 170 180 HADYIKNMIT GAAQMDGAII VVAATDGQMP QTREHLLLAR QVGVQHIVVF VNKVDTIDDP 190 200 210 220 230 240 EMLELVEMEM RELLNEYGFD GDNAPIIMGS ALCALEGRQP EIGEQAIMKL LDAVDEYIPT 250 260 270 280 290 300 PERDLNKPFL MPVEDIFSIS GRGTVVTGRV ERGNLKKGEE LEIVGHNSTP LKTTVTGIEM 310 320 330 340 350 360 FRKELDSAMA GDNAGVLLRG IRRDQLKRGM VLAKPGTVKA HTKILASLYI LSKEEGGRHS 370 380 390 400 410 420 GFGENYRPQM FIRTADVTVV MRFPKEVEDH SMQVMPGDNV EMECDLIHPT PLEVGQRFNI 430 REGGRTVGTG LITRIIE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence determination of the nuclear gene coding for mitochondrial elongation factor Tu of Saccharomyces cerevisiae." Nagata S., Tsunetsugu-Yokota Y., Naito A., Kaziro Y. Proc. Natl. Acad. Sci. U.S.A. 80:6192-6196(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Mitochondrial protein synthesis is required for maintenance of intact mitochondrial genomes in Saccharomyces cerevisiae." Myers A.M., Pape L.K., Tzagoloff A. EMBO J. 4:2087-2092(1985) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Prediction and identification of new natural substrates of the yeast mitochondrial intermediate peptidase." Branda S.S., Isaya G. J. Biol. Chem. 270:27366-27373(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE BY MPP AND MIP, IDENTIFICATION OF PROBABLE CLEAVAGE SITE.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
[9]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100 AND THR-101, MASS SPECTROMETRY.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND THR-296, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	K00428 Genomic DNA. No translation available. Z75095 Genomic DNA. Translation: CAA99396.1. BK006948 Genomic DNA. Translation: DAA10959.1.
PIR	EFBYT. A03520.
RefSeq	NP_014830.1. NM_001183606.1.
3D structure databases
ProteinModelPortal	P02992.
SMR	P02992. Positions 45-437.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4130N.
IntAct	P02992. 13 interactions.
MINT	MINT-497322.
STRING	4932.YOR187W.
Proteomic databases
PaxDb	P02992.
PeptideAtlas	P02992.
PRIDE	P02992.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOR187W; YOR187W; YOR187W.
GeneID	854359.
KEGG	sce:YOR187W.
Organism-specific databases
CYGD	YOR187w.
SGD	S000005713. TUF1.
Phylogenomic databases
eggNOG	COG0050.
GeneTree	ENSGT00550000074682.
HOGENOM	HOG000229290.
KO	K02358.
OMA	CEFVGYN.
OrthoDB	EOG42RHGS.
Enzyme and pathway databases
BioCyc	YEAST:G3O-33697-MONOMER.
UniPathway	UPA00345.
Gene expression databases
Genevestigator	P02992.
GermOnline	YOR187W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000795. EF_GTP-bd_dom. IPR027417. P-loop_NTPase. IPR005225. Small_GTP-bd_dom. IPR009001. Transl_elong_EF1A/Init_IF2_C. IPR004161. Transl_elong_EFTu/EF1A_2. IPR004541. Transl_elong_EFTu/EF1A_bac/org. IPR004160. Transl_elong_EFTu/EF1A_C. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view]
PANTHER	PTHR23115:SF31. PTHR23115:SF31. 1 hit.
Pfam	PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. PF03143. GTP_EFTU_D3. 1 hit. [Graphical view]
PRINTS	PR00315. ELONGATNFCT.
SUPFAM	SSF50465. Elong_init_C. 1 hit. SSF52540. SSF52540. 1 hit. SSF50447. Translat_factor. 1 hit.
TIGRFAMs	TIGR00485. EF-Tu. 1 hit. TIGR00231. small_GTP. 1 hit.
PROSITE	PS00301. EFACTOR_GTP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	976464.

Entry information

Entry name

EFTU_YEAST

Accession

Primary (citable) accession number: P02992
Secondary accession number(s): D6W2P3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 29, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program