※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor G
Protein Synonyms/Alias
 EF-G;  VEG19
Gene Name
 fusA
Gene Synonyms/Alias
 fus; OrderedLocusNames=BSU01120
Created Date
 3-June-2014
Organism
 Bacillus subtilis (strain 168)
NCBI Taxa ID
 224308
Phosphorylation
Position
Peptide
Code
Type
References
24 AHIDAGKTTTTERIL T HTP [1]
302 NEEIERHSSDEEPFS S HTP [1],UniProt
213 QAEELRNSLIEAVCE S HTP [1],UniProt
680 HYEEVPKSVAEEIIK S HTP [1],UniProt
569 KAKLFDGSYHDVDSN S HTP [1],UniProt
48 GETHEGASQMDWMEQ S HTP [1]
43 RIHKIGETHEGASQM T HTP [1]
25 HIDAGKTTTTERILF T HTP [1]
Reference
 [1]The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
 Macek B,Mijakovic I,Olsen JV,Gnad F,Kumar C,Jensen PR,Mann M
 Mol. Cell Proteomics 2007, Apr;6(4):697-707. [PMID:17218307]
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 (By similarity)
Sequence Annotation From UniProt
 MOD_RES 213 213 Phosphoserine
 MOD_RES 302 302 Phosphoserine
 MOD_RES 569 569 Phosphoserine
 MOD_RES 680 680 Phosphoserine
Key Word From UniProt
 Completeproteome; Cytoplasm; Directproteinsequencing; Elongationfactor; GTP-binding; Nucleotide-binding; Phosphoprotein; Proteinbiosynthesis; Referenceproteome
Protein Sequence
 MAREFSLEKT RNIGIMAHID AGKTTTTERI LFYTGRIHKI GETHEGASQM DWMEQEQERG 60
 ITITSAATTA QWKGYRVNII DTPGHVDFTV EVERSLRVLD GAVAVLDAQS GVEPQTETVW 120
 RQATTYGVPR IVFVNKMDKI GADFLYSVGT LRDRLQANAH AIQLPIGAED NFEGIIDLVE 180
 NVAYFYEDDL GTRSDAKEIP EEYKEQAEEL RNSLIEAVCE LDEELMDKYL EGEEITIDEL 240
 KAGIRKGTLN VEFYPVLVGS AFKNKGVQLV LDAVLDYLPA PTDVAAIKGT RPDTNEEIER 300
 HSSDEEPFSA LAFKVMTDPY VGKLTFFRVY SGTLDSGSYV KNSTKGKRER VGRILQMHAN 360
 SREEISTVYA GDIAAAVGLK DTTTGDTLCD EKDLVILESM EFPEPVIDVA IEPKSKADQD 420
 KMGIALAKLA EEDPTFRTQT NPETGQTIIS GMGELHLDII VDRMKREFKV EANVGAPQVA 480
 YRETFRTGAK VEGKFVRQSG GRGQFGHVWI EFEPNEEGAG FEFENAIVGG VVPREYIPAV 540
 QAGLEDALEN GVLAGFPLID IKAKLFDGSY HDVDSNEMAF KVAASMALKN AVSKCNPVLL 600
 EPIMKVEVVI PEEYMGDIMG DITSRRGRVE GMEARGNAQV VRAMVPLAEM FGYATALRSN 660
 TQGRGTFTMH MDHYEEVPKS VAEEIIKKNK GE 692
  GO:0005737   C:cytoplasm IEA:UniProtKB-SubCell
  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.