※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor G
Protein Synonyms/Alias
 EF-G
Gene Name
 fusA
Gene Synonyms/Alias
 far, fus; OrderedLocusNames=b3340, JW3302
Created Date
 3-June-2014
Organism
 Escherichia coli (strain K12)
NCBI Taxa ID
 83333
Phosphorylation
Position
Peptide
Code
Type
References
636 GDVIGDLSRRRGMLK S HTP [1]
692 LKYDEAPSNVAQAVI S HTP [1]
312 TPAERHASDDEPFSA S HTP [2]
509 EGKHAKQSGGRGQYG S HTP [2]
Reference
 [1]Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation.
 Macek B,Gnad F,Soufi B,Kumar C,Olsen JV,Mijakovic I,Mann M
 Mol. Cell Proteomics 2008, Feb;7(2):299-307. [PMID:17938405]
 [2]Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium.
 Soares NC,Spät P,Krug K,Macek B
 J. Proteome Res. 2013, Jun, 7;12(6):2611-21. [PMID:23590516]
Functional Description From UniProt
 FUNCTION: 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
Sequence Annotation From UniProt
 MOD_RES 504 504 N6-acetyllysine
 MOD_RES 643 643 N6-acetyllysine
Key Word From UniProt
 3D-structure; Acetylation; Completeproteome; Cytoplasm; Directproteinsequencing; Elongationfactor; GTP-binding; Nucleotide-binding; Proteinbiosynthesis; Referenceproteome
Protein Sequence
 MARTTPIARY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMEQEQERG 60
 ITITSAATTA FWSGMAKQYE PHRINIIDTP GHVDFTIEVE RSMRVLDGAV MVYCAVGGVQ 120
 PQSETVWRQA NKYKVPRIAF VNKMDRMGAN FLKVVNQIKT RLGANPVPLQ LAIGAEEHFT 180
 GVVDLVKMKA INWNDADQGV TFEYEDIPAD MVELANEWHQ NLIESAAEAS EELMEKYLGG 240
 EELTEAEIKG ALRQRVLNNE IILVTCGSAF KNKGVQAMLD AVIDYLPSPV DVPAINGILD 300
 DGKDTPAERH ASDDEPFSAL AFKIATDPFV GNLTFFRVYS GVVNSGDTVL NSVKAARERF 360
 GRIVQMHANK REEIKEVRAG DIAAAIGLKD VTTGDTLCDP DAPIILERME FPEPVISIAV 420
 EPKTKADQEK MGLALGRLAK EDPSFRVWTD EESNQTIIAG MGELHLDIIV DRMKREFNVE 480
 ANVGKPQVAY RETIRQKVTD VEGKHAKQSG GRGQYGHVVI DMYPLEPGSN PKGYEFINDI 540
 KGGVIPGEYI PAVDKGIQEQ LKAGPLAGYP VVDMGIRLHF GSYHDVDSSE LAFKLAASIA 600
 FKEGFKKAKP VLLEPIMKVE VETPEENTGD VIGDLSRRRG MLKGQESEVT GVKIHAEVPL 660
 SEMFGYATQL RSLTKGRASY TMEFLKYDEA PSNVAQAVIE ARGK 704
  GO:0005737   C:cytoplasm IDA:UniProtKB
  GO:0005525   F:GTP binding IEA:UniProtKB-HAMAP
  GO:0003924   F:GTPase activity IEA:InterPro
  GO:0003746   F:translation elongation factor activity IEA:UniProtKB-HAMAP
  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.
  PF00679   EFG_C.
  PF14492   EFG_II.
  PF03764   EFG_IV.
  PF00009   GTP_EFTU.
  PF03144   GTP_EFTU_D2.
  SM00838   EFG_C.
  SM00889   EFG_IV.
  PS00301   EFACTOR_GTP.
  PR00315   ELONGATNFCT.