Elongation factor Tu
Details
- Name
- Elongation factor Tu
- Kind
- protein
- Synonyms
- EF-Tu
- tufA
- Gene Name
- tuf
- UniProtKB Entry
- Q01698Swiss-Prot
- Organism
- Thermus aquaticus
- NCBI Taxonomy ID
- 271
- Amino acid sequence
>lcl|BSEQ0012288|Elongation factor Tu MAKGEFIRTKPHVNVGTIGHVDHGKTTLTAALTYVAAAENPNVEVKDYGDIDKAPEERAR GITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAILVVSAADGPMPQTREH ILLARQVGVPYIVVFMNKVDMVDDPELLDLVEMEVRDLLNQYEFPGDEVPVIRGSALLAL EEMHKNPKTKRGENEWVDKIWELLDAIDEYIPTPVRDVDKPFLMPVEDVFTITGRGTVAT GRIERGKVKVGDEVEIVGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVE RGQVLAKPGSITPHTKFEASVYILKKEEGGRHTGFFTGYRPQFYFRTTDVTGVVRLPQGV EMVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVVTKILE
- Number of residues
- 406
- Molecular Weight
- 44814.085
- Theoretical pI
- 5.36
- GO Classification
- FunctionsGTP binding / GTPase activity / translation elongation factor activityComponentscytoplasm
- General Function
- This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
- Specific Function
- GTP binding
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0006394|1221 bp ATGGCGAAGGGCGAGTTTATCCGGACGAAGCCCCACGTGAACGTGGGGACGATTGGGCAC GTGGACCACGGGAAGACGACGTTGACGGCGGCCTTGACCTATGTGGCGGCGGCGGAGAAC CCGAATGTGGAGGTGAAGGACTACGGGGACATTGACAAGGCGCCGGAGGAGCGGGCGCGG GGGATCACGATTAACACGGCGCACGTGGAGTACGAGACGGCGAAGCGGCACTATTCCCAC GTGGACTGCCCGGGGCACGCCGACTACATCAAGAACATGATCACCGGGGCGGCGCAGATG GACGGGGCGATCCTGGTGGTTTCTGCGGCGGACGGTCCTATGCCGCAGACCCGGGAGCAC ATTCTTTTGGCCCGCCAGGTGGGGGTGCCGTACATCGTGGTGTTCATGAACAAGGTGGAC ATGGTGGACGACCCGGAGCTCTTGGACCTGGTGGAGATGGAGGTGAGGGACCTCCTGAAC CAGTACGAGTTTCCTGGGGACGAGGTGCCGGTGATCCGGGGTAGCGCCCTGCTTGCGTTG GAAGAGATGCACAAGAACCCGAAGACCAAGCGGGGCGAGAACGAGTGGGTGGACAAGATC TGGGAGCTTTTGGACGCCATTGACGAGTACATTCCCACGCCGGTGCGGGACGTGGACAAG CCTTTCCTGATGCCGGTGGAGGACGTGTTTACGATTACCGGGCGTGGGACGGTGGCCACC GGGCGGATTGAGCGGGGCAAGGTGAAGGTTGGGGACGAGGTGGAGATCGTGGGCCTGGCT CCGGAGACGCGGAAGACGGTGGTCACGGGTGTGGAGATGCACCGGAAGACGTTGCAGGAG GGGATCGCTGGGGACAACGTGGGTCTTCTTCTGCGGGGCGTGAGCCGGGAGGAGGTGGAG CGGGGGCAGGTATTGGCCAAGCCTGGGAGCATCACGCCGCACACCAAGTTTGAGGCCTCG GTGTACATCCTGAAGAAGGAGGAGGGCGGGCGGCACACGGGGTTTTTCACGGGGTACCGG CCGCAGTTTTACTTCCGGACGACGGACGTGACGGGGGTGGTGCGGTTGCCCCAGGGGGTG GAGATGGTGATGCCTGGGGACAACGTGACCTTCACGGTGGAGCTCATCAAGCCGGTGGCG CTGGAGGAGGGTTTGCGGTTTGCCATCCGGGAGGGTGGGCGGACCGTGGGCGCCGGCGTG GTCACCAAGATCCTGGAGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q01698 UniProtKB Entry Name EFTU_THEAQ GenBank Gene ID X66322 PDB ID(s) 1B23, 1EFT, 1H1U, 1IPM, 1IPO, 1IPQ, 1IPR, 1IPU, 1L1U, 1MJ1, 1OB5, 1TTT, 1TUI - General References
- Voss RH, Hartmann RK, Lippmann C, Alexander C, Jahn O, Erdmann VA: Sequence of the tufA gene encoding elongation factor EF-Tu from Thermus aquaticus and overproduction of the protein in Escherichia coli. Eur J Biochem. 1992 Aug 1;207(3):839-46. [Article]
- Kjeldgaard M, Nissen P, Thirup S, Nyborg J: The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure. 1993 Sep 15;1(1):35-50. [Article]
- Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark BF, Nyborg J: Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science. 1995 Dec 1;270(5241):1464-72. [Article]
- Polekhina G, Thirup S, Kjeldgaard M, Nissen P, Lippmann C, Nyborg J: Helix unwinding in the effector region of elongation factor EF-Tu-GDP. Structure. 1996 Oct 15;4(10):1141-51. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Guanosine-5'-Diphosphate experimental unknown target Details 2-METHYLTHIO-N6-ISOPENTENYL-ADENOSINE-5'-MONOPHOSPHATE experimental unknown target Details