Elongation factor G - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0A6M8 (EFG_ECOLI)

Last modified June 16, 2009. Version 45. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Elongation factor G
Short name=EF-G

Gene names

Name:	fusA
Synonyms:	far, fus
Ordered Locus Names:	b3340, JW3302

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	704 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	This protein promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome. HAMAP MF_00054
Subcellular location	Cytoplasm. HAMAP MF_00054
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.

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Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	translational elongation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	GTP binding Inferred from electronic annotation. Source: HAMAP GTPase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct translation elongation factor activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
thrC	P00934	1	EBI-370503,EBI-1112675

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5 Ref.8

Chain

2 – 704

703

Elongation factor G HAMAP MF_00054

PRO_0000091119

Regions

Nucleotide binding

17 – 24

GTP By similarity

Nucleotide binding

88 – 92

GTP By similarity

Nucleotide binding

142 – 145

GTP By similarity

Amino acid modifications

Modified residue

504

N6-acetyllysine Ref.11

Modified residue

643

N6-acetyllysine Ref.11

Experimental info

Sequence conflict

296 – 297

NG → DC AA sequence Ref.5

Sequence conflict

300 – 302

Missing AA sequence Ref.5

Sequence conflict

396

T → C AA sequence Ref.5

Sequence conflict

576

I → V AA sequence Ref.5

Sequence conflict

576

I → V AA sequence Ref.9

Sequence conflict

584

H → K AA sequence Ref.5

Sequence conflict

584

H → K AA sequence Ref.9

Sequence conflict

594

K → H AA sequence Ref.5

Sequence conflict

594

K → H AA sequence Ref.9

Sequence conflict

626

E → Q AA sequence Ref.5

Sequence conflict

626

E → Q AA sequence Ref.9

Sequence conflict

646

E → Q AA sequence Ref.5

Sequence conflict

646

E → Q AA sequence Ref.9

Sequence conflict

657

E → Q AA sequence Ref.5

Sequence conflict

657

E → Q AA sequence Ref.9

Sequence conflict

662

E → EQ AA sequence Ref.5

Sequence conflict

662

E → EQ AA sequence Ref.9

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A6M8-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8C72B9F87253BC7B
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FASTA

704

77,581

        10         20         30         40         50         60 
MARTTPIARY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMEQEQERG 

        70         80         90        100        110        120 
ITITSAATTA FWSGMAKQYE PHRINIIDTP GHVDFTIEVE RSMRVLDGAV MVYCAVGGVQ 

       130        140        150        160        170        180 
PQSETVWRQA NKYKVPRIAF VNKMDRMGAN FLKVVNQIKT RLGANPVPLQ LAIGAEEHFT 

       190        200        210        220        230        240 
GVVDLVKMKA INWNDADQGV TFEYEDIPAD MVELANEWHQ NLIESAAEAS EELMEKYLGG 

       250        260        270        280        290        300 
EELTEAEIKG ALRQRVLNNE IILVTCGSAF KNKGVQAMLD AVIDYLPSPV DVPAINGILD 

       310        320        330        340        350        360 
DGKDTPAERH ASDDEPFSAL AFKIATDPFV GNLTFFRVYS GVVNSGDTVL NSVKAARERF 

       370        380        390        400        410        420 
GRIVQMHANK REEIKEVRAG DIAAAIGLKD VTTGDTLCDP DAPIILERME FPEPVISIAV 

       430        440        450        460        470        480 
EPKTKADQEK MGLALGRLAK EDPSFRVWTD EESNQTIIAG MGELHLDIIV DRMKREFNVE 

       490        500        510        520        530        540 
ANVGKPQVAY RETIRQKVTD VEGKHAKQSG GRGQYGHVVI DMYPLEPGSN PKGYEFINDI 

       550        560        570        580        590        600 
KGGVIPGEYI PAVDKGIQEQ LKAGPLAGYP VVDMGIRLHF GSYHDVDSSE LAFKLAASIA 

       610        620        630        640        650        660 
FKEGFKKAKP VLLEPIMKVE VETPEENTGD VIGDLSRRRG MLKGQESEVT GVKIHAEVPL 

       670        680        690        700 
SEMFGYATQL RSLTKGRASY TMEFLKYDEA PSNVAQAVIE ARGK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of the Escherichia coli fus gene, coding for elongation factor G." Zengel J.M., Archer R.H., Lindahl L. Nucleic Acids Res. 12:2181-2192(1984) [PubMed: 6322136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Comparison of the complete sequence of the str operon in Salmonella typhimurium and Escherichia coli." Johanson U., Hughes D. Gene 120:93-98(1992) [PubMed: 1398129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The primary structure of elongation factor G from Escherichia coli. A complete amino acid sequence." Ovchinnikov Y.A., Alakhov Y.B., Bundulis Y.P., Bundule M.A., Dovgas N.V., Kozlov V.P., Motuz L.P., Vinokurov L.M. FEBS Lett. 139:130-135(1982) [PubMed: 7042386] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-704.
[6]	"DNA sequences from the str operon of Escherichia coli." Post L.E., Nomura M. J. Biol. Chem. 255:4660-4666(1980) [PubMed: 6989816] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94. Strain: K12.
[7]	Weigel C.T.O. Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. Strain: L44.
[8]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[9]	"The primary structure of the elongation factor G from Escherichia coli: amino acid sequence of the C-terminal domain." Alakhov Y.B., Dovgas N.V., Motuz L.P., Vinokurov L.M., Ovchinnikov Y.A. FEBS Lett. 126:183-186(1981) [PubMed: 7016587] [Abstract] Cited for: PROTEIN SEQUENCE OF 476-702.
[10]	"The nucleotide sequence of the cloned tufA gene of Escherichia coli." Yokota T., Sugisaki H., Takanami M., Kaziro Y. Gene 12:25-31(1980) [PubMed: 7011903] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 684-704.
[11]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-504 AND LYS-643, MASS SPECTROMETRY.
[12]	"Locking and unlocking of ribosomal motions." Valle M., Zavialov A., Sengupta J., Rawat U., Ehrenberg M., Frank J. Cell 114:123-134(2003) [PubMed: 12859903] [Abstract] Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES WITH EF-G.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X00415 Genomic DNA. Translation: CAA25120.1.
X64592 Genomic DNA. No translation available.
U18997 Genomic DNA. Translation: AAA58137.1.
U00096 Genomic DNA. Translation: AAC76365.1.
AP009048 Genomic DNA. Translation: BAE77951.1.
J01689 Genomic DNA. Translation: AAA50991.1.
X65735 Genomic DNA. Translation: CAA46645.1.

PIR

EFECG. G65127.

RefSeq

AP_004450.1.
NP_417799.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RDO	electron microscopy	9.10	7	1-704	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6M8. 41 interactions.

PTM databases

PhosSite

P0A6M8.

2-D gel databases

SWISS-2DPAGE

P0A6M8.

2DBase-Ecoli

P0A6M8.

ECO2DBASE

D084.0. 6TH EDITION.

Genome annotation databases

GeneID

947847.

GenomeReviews

Gene locus JW3302 in contig AP009048_GR.
Gene locus b3340 in contig U00096_GR.

KEGG

ecj:JW3302.
eco:b3340.

Organism-specific databases

EchoBASE

EB0355.

EcoGene

EG10360. fusA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A6M8.

OMA

P0A6M8. HPLILES.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10360-MON.

Family and domain databases

HAMAP

MF_00054.
[Tree]

InterPro

IPR000795. ProtSyn_GTP_bd.
IPR014721. Ribosomal_S5_D2-type_fold.
IPR005225. Small_GTP_bd.
IPR004540. Transl_elong_EFG/EF2.
IPR000640. Transl_elong_EFG/EF2_C.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]

Gene3D

G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
G3DSA:3.30.70.240. Transl_elong_EFG/EF2_C. 1 hit.

Pfam

PF00679. EFG_C. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]

PRINTS

PR00315. ELONGATNFCT.

TIGRFAMs

TIGR00484. EF-G. 1 hit.
TIGR00231. small_GTP. 1 hit.

PROSITE

PS00301. EFACTOR_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

EFG_ECOLI

Accession

Primary (citable) accession number: P0A6M8
Secondary accession number(s): P02996, Q2M705, Q9F439

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents