Elongation factor G
Details
- Name
- Elongation factor G
- Synonyms
- EF-G
- fus
- Gene Name
- fusA
- Organism
- Thermus thermophilus
- Amino acid sequence
>lcl|BSEQ0019178|Elongation factor G MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPV ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ
- Number of residues
- 691
- Molecular Weight
- 76878.69
- Theoretical pI
- 5.09
- GO Classification
- FunctionsGTP binding / GTPase activity / translation elongation factor activityComponentscytoplasm
- General Function
- Translation elongation factor activity
- Specific 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.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P13551 UniProtKB Entry Name EFG_THETH - General References
- al-Karadaghi S, Aevarsson A, Garber M, Zheltonosova J, Liljas A: The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. Structure. 1996 May 15;4(5):555-65. [Article]
- Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A: Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. J Mol Biol. 2000 Nov 3;303(4):593-603. [Article]