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Protein

Elongation factor G

Gene

fusA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Nucleotide bindingi17 – 24GTPBy similarity8
Nucleotide bindingi88 – 92GTPBy similarity5
Nucleotide bindingi142 – 145GTPBy similarity4

GO - Molecular functioni

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10360. fusA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000911192 – 704Elongation factor GAdd BLAST703

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei504N6-acetyllysine1 Publication1
Modified residuei643N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A6M8.
PaxDbiP0A6M8.
PRIDEiP0A6M8.

2D gel databases

SWISS-2DPAGEP0A6M8.

Interactioni

Protein-protein interaction databases

BioGridi4259389. 48 interactors.
DIPiDIP-31836N.
IntActiP0A6M8. 42 interactors.
STRINGi511145.b3340.

Structurei

Secondary structure

1704
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 16Combined sources7
Beta strandi18 – 20Combined sources3
Turni21 – 24Combined sources4
Helixi25 – 34Combined sources10
Helixi54 – 58Combined sources5
Beta strandi66 – 72Combined sources7
Beta strandi82 – 88Combined sources7
Beta strandi92 – 95Combined sources4
Helixi97 – 104Combined sources8
Beta strandi107 – 117Combined sources11
Helixi121 – 132Combined sources12
Beta strandi138 – 142Combined sources5
Helixi151 – 160Combined sources10
Beta strandi166 – 175Combined sources10
Beta strandi178 – 184Combined sources7
Turni185 – 188Combined sources4
Beta strandi195 – 199Combined sources5
Turni209 – 211Combined sources3
Helixi212 – 215Combined sources4
Helixi220 – 227Combined sources8
Helixi231 – 238Combined sources8
Helixi245 – 256Combined sources12
Turni257 – 259Combined sources3
Beta strandi262 – 264Combined sources3
Turni269 – 272Combined sources4
Helixi275 – 285Combined sources11
Beta strandi289 – 292Combined sources4
Beta strandi300 – 302Combined sources3
Beta strandi318 – 327Combined sources10
Turni328 – 330Combined sources3
Beta strandi331 – 344Combined sources14
Beta strandi348 – 351Combined sources4
Turni352 – 355Combined sources4
Beta strandi356 – 359Combined sources4
Beta strandi363 – 366Combined sources4
Beta strandi368 – 378Combined sources11
Beta strandi382 – 386Combined sources5
Beta strandi396 – 399Combined sources4
Beta strandi400 – 402Combined sources3
Beta strandi416 – 421Combined sources6
Helixi425 – 427Combined sources3
Helixi428 – 441Combined sources14
Beta strandi446 – 449Combined sources4
Beta strandi451 – 453Combined sources3
Beta strandi456 – 462Combined sources7
Helixi463 – 477Combined sources15
Beta strandi482 – 484Combined sources3
Beta strandi491 – 496Combined sources6
Beta strandi498 – 504Combined sources7
Beta strandi509 – 512Combined sources4
Beta strandi517 – 524Combined sources8
Turni529 – 532Combined sources4
Beta strandi533 – 537Combined sources5
Beta strandi542 – 545Combined sources4
Turni547 – 549Combined sources3
Helixi550 – 560Combined sources11
Beta strandi562 – 564Combined sources3
Turni565 – 567Combined sources3
Beta strandi573 – 582Combined sources10
Beta strandi585 – 587Combined sources3
Helixi590 – 604Combined sources15
Helixi606 – 608Combined sources3
Beta strandi610 – 623Combined sources14
Helixi625 – 627Combined sources3
Helixi628 – 637Combined sources10
Beta strandi641 – 644Combined sources4
Beta strandi651 – 660Combined sources10
Helixi666 – 673Combined sources8
Turni674 – 676Combined sources3
Beta strandi680 – 689Combined sources10
Helixi692 – 697Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RDOelectron microscopy9.1071-704[»]
3J0Eelectron microscopy9.90H2-703[»]
3J9Zelectron microscopy3.60S12-703[»]
3JA1electron microscopy3.60S32-703[»]
4V7Belectron microscopy6.80AY1-704[»]
4V7Delectron microscopy7.60BZ2-704[»]
4V9OX-ray2.90BV/DV/FV/HV1-704[»]
4V9PX-ray2.90BV/DV/FV/HV1-704[»]
ProteinModelPortaliP0A6M8.
SMRiP0A6M8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6M8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 290tr-type GAdd BLAST283

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CEJ. Bacteria.
COG0480. LUCA.
HOGENOMiHOG000231585.
InParanoidiP0A6M8.
KOiK02355.
OMAiKLGVAIQ.
PhylomeDBiP0A6M8.

Family and domain databases

CDDicd01434. EFG_mtEFG1_IV. 1 hit.
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. 1 hit.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 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)DescriptionActionsGraphical viewLength
Sequence conflicti296 – 297NG → DC AA sequence (PubMed:7042386).Curated2
Sequence conflicti300 – 302Missing AA sequence (PubMed:7042386).Curated3
Sequence conflicti396T → C AA sequence (PubMed:7042386).Curated1
Sequence conflicti576I → V AA sequence (PubMed:7042386).Curated1
Sequence conflicti576I → V AA sequence (PubMed:7016587).Curated1
Sequence conflicti584H → K AA sequence (PubMed:7042386).Curated1
Sequence conflicti584H → K AA sequence (PubMed:7016587).Curated1
Sequence conflicti594K → H AA sequence (PubMed:7042386).Curated1
Sequence conflicti594K → H AA sequence (PubMed:7016587).Curated1
Sequence conflicti626E → Q AA sequence (PubMed:7042386).Curated1
Sequence conflicti626E → Q AA sequence (PubMed:7016587).Curated1
Sequence conflicti646E → Q AA sequence (PubMed:7042386).Curated1
Sequence conflicti646E → Q AA sequence (PubMed:7016587).Curated1
Sequence conflicti657E → Q AA sequence (PubMed:7042386).Curated1
Sequence conflicti657E → Q AA sequence (PubMed:7016587).Curated1
Sequence conflicti662E → EQ AA sequence (PubMed:7042386).Curated1
Sequence conflicti662E → EQ AA sequence (PubMed:7016587).Curated1

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.
WP_000124700.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76365; AAC76365; b3340.
BAE77951; BAE77951; BAE77951.
GeneIDi947847.
KEGGiecj:JW3302.
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.
PIRiG65127. EFECG.
RefSeqiNP_417799.1. NC_000913.3.
WP_000124700.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RDOelectron microscopy9.1071-704[»]
3J0Eelectron microscopy9.90H2-703[»]
3J9Zelectron microscopy3.60S12-703[»]
3JA1electron microscopy3.60S32-703[»]
4V7Belectron microscopy6.80AY1-704[»]
4V7Delectron microscopy7.60BZ2-704[»]
4V9OX-ray2.90BV/DV/FV/HV1-704[»]
4V9PX-ray2.90BV/DV/FV/HV1-704[»]
ProteinModelPortaliP0A6M8.
SMRiP0A6M8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259389. 48 interactors.
DIPiDIP-31836N.
IntActiP0A6M8. 42 interactors.
STRINGi511145.b3340.

2D gel databases

SWISS-2DPAGEP0A6M8.

Proteomic databases

EPDiP0A6M8.
PaxDbiP0A6M8.
PRIDEiP0A6M8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76365; AAC76365; b3340.
BAE77951; BAE77951; BAE77951.
GeneIDi947847.
KEGGiecj:JW3302.
eco:b3340.
PATRICi32122112. VBIEscCol129921_3433.

Organism-specific databases

EchoBASEiEB0355.
EcoGeneiEG10360. fusA.

Phylogenomic databases

eggNOGiENOG4105CEJ. Bacteria.
COG0480. LUCA.
HOGENOMiHOG000231585.
InParanoidiP0A6M8.
KOiK02355.
OMAiKLGVAIQ.
PhylomeDBiP0A6M8.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A6M8.
PROiP0A6M8.

Family and domain databases

CDDicd01434. EFG_mtEFG1_IV. 1 hit.
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. 1 hit.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 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]
ProtoNetiSearch...

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 2, 2016
This is version 108 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.