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P0A6M8

- EFG_ECOLI

UniProt

P0A6M8 - EFG_ECOLI

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Protein

Elongation factor G

Gene

fusA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 248GTPBy similarity
Nucleotide bindingi88 – 925GTPBy similarity
Nucleotide bindingi142 – 1454GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-HAMAP
  3. translation elongation factor activity Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10360-MONOMER.
ECOL316407:JW3302-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor G
Short name:
EF-G
Gene namesi
Name:fusA
Synonyms:far, fus
Ordered Locus Names:b3340, JW3302
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10360. fusA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 704703Elongation factor GPRO_0000091119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei504 – 5041N6-acetyllysine1 Publication
Modified residuei643 – 6431N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A6M8.
PRIDEiP0A6M8.

2D gel databases

SWISS-2DPAGEP0A6M8.

PTM databases

PhosSiteiP0809388.

Expressioni

Gene expression databases

GenevestigatoriP0A6M8.

Interactioni

Protein-protein interaction databases

DIPiDIP-31836N.
IntActiP0A6M8. 42 interactions.
STRINGi511145.b3340.

Structurei

Secondary structure

1
704
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 167Combined sources
Beta strandi18 – 203Combined sources
Turni21 – 244Combined sources
Helixi25 – 3410Combined sources
Helixi54 – 585Combined sources
Beta strandi66 – 727Combined sources
Beta strandi82 – 887Combined sources
Beta strandi92 – 954Combined sources
Helixi97 – 1048Combined sources
Beta strandi107 – 11711Combined sources
Helixi121 – 13212Combined sources
Beta strandi138 – 1425Combined sources
Helixi151 – 16010Combined sources
Beta strandi166 – 17510Combined sources
Beta strandi178 – 1847Combined sources
Turni185 – 1884Combined sources
Beta strandi195 – 1995Combined sources
Turni209 – 2113Combined sources
Helixi212 – 2154Combined sources
Helixi220 – 2278Combined sources
Helixi231 – 2388Combined sources
Helixi245 – 25612Combined sources
Turni257 – 2593Combined sources
Beta strandi262 – 2643Combined sources
Turni269 – 2724Combined sources
Helixi275 – 28511Combined sources
Beta strandi289 – 2924Combined sources
Beta strandi300 – 3023Combined sources
Beta strandi318 – 32710Combined sources
Turni328 – 3303Combined sources
Beta strandi331 – 34414Combined sources
Beta strandi348 – 3514Combined sources
Turni352 – 3554Combined sources
Beta strandi356 – 3594Combined sources
Beta strandi363 – 3664Combined sources
Beta strandi368 – 37811Combined sources
Beta strandi382 – 3865Combined sources
Beta strandi396 – 3994Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi416 – 4216Combined sources
Helixi425 – 4273Combined sources
Helixi428 – 44114Combined sources
Beta strandi446 – 4494Combined sources
Beta strandi451 – 4533Combined sources
Beta strandi456 – 4627Combined sources
Helixi463 – 47715Combined sources
Beta strandi482 – 4843Combined sources
Beta strandi491 – 4966Combined sources
Beta strandi498 – 5047Combined sources
Beta strandi509 – 5124Combined sources
Beta strandi517 – 5248Combined sources
Turni529 – 5324Combined sources
Beta strandi533 – 5375Combined sources
Beta strandi542 – 5454Combined sources
Turni547 – 5493Combined sources
Helixi550 – 56011Combined sources
Beta strandi562 – 5643Combined sources
Turni565 – 5673Combined sources
Beta strandi573 – 58210Combined sources
Beta strandi585 – 5873Combined sources
Helixi590 – 60415Combined sources
Helixi606 – 6083Combined sources
Beta strandi610 – 62314Combined sources
Helixi625 – 6273Combined sources
Helixi628 – 63710Combined sources
Beta strandi641 – 6444Combined sources
Beta strandi651 – 66010Combined sources
Helixi666 – 6738Combined sources
Turni674 – 6763Combined sources
Beta strandi680 – 68910Combined sources
Helixi692 – 6976Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RDOelectron microscopy9.1071-704[»]
3J0Eelectron microscopy9.90H2-703[»]
3J5Nelectron microscopy6.80Y1-704[»]
3J5Xelectron microscopy7.60Z2-704[»]
4KIYX-ray2.90V1-704[»]
4KJ0X-ray2.90V1-704[»]
4KJ2X-ray2.90V1-704[»]
4KJ4X-ray2.90V1-704[»]
4KJ6X-ray2.90V1-704[»]
4KJ8X-ray2.90V1-704[»]
4KJAX-ray2.90V1-704[»]
4KJCX-ray2.90V1-704[»]
ProteinModelPortaliP0A6M8.
SMRiP0A6M8. Positions 2-703.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6M8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 290283tr-type GAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0480.
HOGENOMiHOG000231585.
InParanoidiP0A6M8.
KOiK02355.
OMAiSGVQPQT.
OrthoDBiEOG6X6RBF.
PhylomeDBiP0A6M8.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00054_B. EF_G_EF_2_B.
InterProiIPR000795. 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.
IPR009000. Transl_B-barrel.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00484. EF-G. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6M8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARTTPIARY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM
60 70 80 90 100
DWMEQEQERG ITITSAATTA FWSGMAKQYE PHRINIIDTP GHVDFTIEVE
110 120 130 140 150
RSMRVLDGAV MVYCAVGGVQ PQSETVWRQA NKYKVPRIAF VNKMDRMGAN
160 170 180 190 200
FLKVVNQIKT RLGANPVPLQ LAIGAEEHFT GVVDLVKMKA INWNDADQGV
210 220 230 240 250
TFEYEDIPAD MVELANEWHQ NLIESAAEAS EELMEKYLGG EELTEAEIKG
260 270 280 290 300
ALRQRVLNNE IILVTCGSAF KNKGVQAMLD AVIDYLPSPV DVPAINGILD
310 320 330 340 350
DGKDTPAERH ASDDEPFSAL AFKIATDPFV GNLTFFRVYS GVVNSGDTVL
360 370 380 390 400
NSVKAARERF GRIVQMHANK REEIKEVRAG DIAAAIGLKD VTTGDTLCDP
410 420 430 440 450
DAPIILERME FPEPVISIAV EPKTKADQEK MGLALGRLAK EDPSFRVWTD
460 470 480 490 500
EESNQTIIAG MGELHLDIIV DRMKREFNVE ANVGKPQVAY RETIRQKVTD
510 520 530 540 550
VEGKHAKQSG GRGQYGHVVI DMYPLEPGSN PKGYEFINDI KGGVIPGEYI
560 570 580 590 600
PAVDKGIQEQ LKAGPLAGYP VVDMGIRLHF GSYHDVDSSE LAFKLAASIA
610 620 630 640 650
FKEGFKKAKP VLLEPIMKVE VETPEENTGD VIGDLSRRRG MLKGQESEVT
660 670 680 690 700
GVKIHAEVPL SEMFGYATQL RSLTKGRASY TMEFLKYDEA PSNVAQAVIE

ARGK
Length:704
Mass (Da):77,581
Last modified:January 23, 2007 - v2
Checksum:i8C72B9F87253BC7B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti296 – 2972NG → DC AA sequence (PubMed:7042386)Curated
Sequence conflicti300 – 3023Missing AA sequence (PubMed:7042386)Curated
Sequence conflicti396 – 3961T → C AA sequence (PubMed:7042386)Curated
Sequence conflicti576 – 5761I → V AA sequence (PubMed:7042386)Curated
Sequence conflicti576 – 5761I → V AA sequence (PubMed:7016587)Curated
Sequence conflicti584 – 5841H → K AA sequence (PubMed:7042386)Curated
Sequence conflicti584 – 5841H → K AA sequence (PubMed:7016587)Curated
Sequence conflicti594 – 5941K → H AA sequence (PubMed:7042386)Curated
Sequence conflicti594 – 5941K → H AA sequence (PubMed:7016587)Curated
Sequence conflicti626 – 6261E → Q AA sequence (PubMed:7042386)Curated
Sequence conflicti626 – 6261E → Q AA sequence (PubMed:7016587)Curated
Sequence conflicti646 – 6461E → Q AA sequence (PubMed:7042386)Curated
Sequence conflicti646 – 6461E → Q AA sequence (PubMed:7016587)Curated
Sequence conflicti657 – 6571E → Q AA sequence (PubMed:7042386)Curated
Sequence conflicti657 – 6571E → Q AA sequence (PubMed:7016587)Curated
Sequence conflicti662 – 6621E → EQ AA sequence (PubMed:7042386)Curated
Sequence conflicti662 – 6621E → EQ AA sequence (PubMed:7016587)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiG65127. EFECG.
RefSeqiNP_417799.1. NC_000913.3.
YP_492092.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76365; AAC76365; b3340.
BAE77951; BAE77951; BAE77951.
GeneIDi12930395.
947847.
KEGGiecj:Y75_p3836.
eco:b3340.
PATRICi32122112. VBIEscCol129921_3433.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi G65127. EFECG.
RefSeqi NP_417799.1. NC_000913.3.
YP_492092.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2RDO electron microscopy 9.10 7 1-704 [» ]
3J0E electron microscopy 9.90 H 2-703 [» ]
3J5N electron microscopy 6.80 Y 1-704 [» ]
3J5X electron microscopy 7.60 Z 2-704 [» ]
4KIY X-ray 2.90 V 1-704 [» ]
4KJ0 X-ray 2.90 V 1-704 [» ]
4KJ2 X-ray 2.90 V 1-704 [» ]
4KJ4 X-ray 2.90 V 1-704 [» ]
4KJ6 X-ray 2.90 V 1-704 [» ]
4KJ8 X-ray 2.90 V 1-704 [» ]
4KJA X-ray 2.90 V 1-704 [» ]
4KJC X-ray 2.90 V 1-704 [» ]
ProteinModelPortali P0A6M8.
SMRi P0A6M8. Positions 2-703.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31836N.
IntActi P0A6M8. 42 interactions.
STRINGi 511145.b3340.

PTM databases

PhosSitei P0809388.

2D gel databases

SWISS-2DPAGE P0A6M8.

Proteomic databases

PaxDbi P0A6M8.
PRIDEi P0A6M8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76365 ; AAC76365 ; b3340 .
BAE77951 ; BAE77951 ; BAE77951 .
GeneIDi 12930395.
947847.
KEGGi ecj:Y75_p3836.
eco:b3340.
PATRICi 32122112. VBIEscCol129921_3433.

Organism-specific databases

EchoBASEi EB0355.
EcoGenei EG10360. fusA.

Phylogenomic databases

eggNOGi COG0480.
HOGENOMi HOG000231585.
InParanoidi P0A6M8.
KOi K02355.
OMAi SGVQPQT.
OrthoDBi EOG6X6RBF.
PhylomeDBi P0A6M8.

Enzyme and pathway databases

BioCyci EcoCyc:EG10360-MONOMER.
ECOL316407:JW3302-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A6M8.
PROi P0A6M8.

Gene expression databases

Genevestigatori P0A6M8.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_00054_B. EF_G_EF_2_B.
InterProi 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.
IPR009000. Transl_B-barrel.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view ]
Pfami PF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SMARTi SM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view ]
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsi TIGR00484. EF-G. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEi PS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 684-704.
  11. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  12. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-504 AND LYS-643, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  13. Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES WITH EF-G.

Entry informationi

Entry nameiEFG_ECOLI
AccessioniPrimary (citable) accession number: P0A6M8
Secondary accession number(s): P02996, Q2M705, Q9F439
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3