※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor Tu 1
Protein Synonyms/Alias
 EF-Tu 1
Gene Name
 tufA
Gene Synonyms/Alias
 b3339, JW3301
Created Date
 3-June-2014
Organism
 Escherichia coli (strain K12)
NCBI Taxa ID
 83333
Phosphorylation
Position
Peptide
Code
Type
References
174 DTPIVRGSALKALEG S HTP [1]
65 ARGITINTSHVEYDT T HTP [1]
222 IEDVFSISGRGTVVT S HTP [1]
168 YDFPGDDTPIVRGSA T HTP [1]
66 RGITINTSHVEYDTP S HTP [1]
313 ESEVYILSKDEGGRH S HTP [1]
332 KGYRPQFYFRTTDVT Y HTP [1]
159 MEVRELLSQYDFPGD S HTP [1]
62 EEKARGITINTSHVE T HTP [1]
198 ELAGFLDSYIPEPER S HTP [2]
310 TKFESEVYILSKDEG Y HTP [2]
39 ITTVLAKTYGGAARA T HTP [2]
161 VRELLSQYDFPGDDT Y HTP [3]
77 YDTPTRHYAHVDCPG Y HTP [3]
88 DCPGHADYVKNMITG Y HTP [3]
70 INTSHVEYDTPTRHY Y HTP [3]
383 AIREGGRTVGAGVVA T LTP [4],UniProt
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]
 [3]The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence.
 Hansen AM,Chaerkady R,Sharma J,Díaz-Mejía JJ,Tyagi N,Renuse S,Jacob HK,Pinto SM,Sahasrabuddhe NA,Kim MS,Delanghe B,Srinivasan N,Emili A,Kaper JB,Pandey A
 PLoS Pathog. 2013;9(6):e1003403. [PMID:23785281]
 [4]Prokaryotic elongation factor Tu is phosphorylated in vivo.
 Lippmann C,Lindschau C,Vijgenboom E,Schröder W,Bosch L,Erdmann VA
 J. Biol. Chem. 1993, Jan, 5;268(1):601-7. [PMID:8416965]
Functional Description From UniProt
 FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis
Sequence Annotation From UniProt
 MOD_RES 2 2 N-acetylserine
 MOD_RES 57 57 N6,N6-dimethyllysine; alternate
 MOD_RES 57 57 N6-methyllysine; alternate
 MOD_RES 314 314 N6-acetyllysine
 MOD_RES 383 383 Phosphothreonine
Key Word From UniProt
 3D-structure; Acetylation; Antibioticresistance; Cellinnermembrane; Cellmembrane; Completeproteome; Cytoplasm; Directproteinsequencing; Elongationfactor; GTP-binding; Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Proteinbiosynthesis; Referenceproteome
Protein Sequence
 MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG 60
 ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI 120
 LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE 180
 GDAEWEAKIL ELAGFLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG 240
 EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK 300
 PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV 360
 VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLG 394
  GO:0005737   C:cytoplasm IDA:UniProtKB
  GO:0005886   C:plasma membrane 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
  GO:0046677   P:response to antibiotic IEA:UniProtKB-KW
  IPR000795   EF_GTP-bd_dom.
  IPR027417   P-loop_NTPase.
  IPR005225   Small_GTP-bd_dom.
  IPR009000   Transl_B-barrel.
  IPR009001   Transl_elong_EF1A/Init_IF2_C.
  IPR004161   Transl_elong_EFTu/EF1A_2.
  IPR004541   Transl_elong_EFTu/EF1A_bac/org.
  IPR004160   Transl_elong_EFTu/EF1A_C.
  PF00009   GTP_EFTU.
  PF03144   GTP_EFTU_D2.
  PF03143   GTP_EFTU_D3.
  PS00301   EFACTOR_GTP.
  PR00315   ELONGATNFCT.