CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002855
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor G 
Protein Synonyms/Alias
 EF-G 
Gene Name
 fusA 
Gene Synonyms/Alias
 STM3446 
Created Date
 July 27, 2013 
Organism
 Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 
NCBI Taxa ID
 99287 
Lysine Modification
Position
Peptide
Type
References
273CGSAFKNKGVQAMLDacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 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
 NP_BIND 17 24 GTP (By similarity).
 NP_BIND 88 92 GTP (By similarity).
 NP_BIND 142 145 GTP (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 704 AA 
Protein Sequence
MARTTPIARY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMEQEQERG 60
ITITSAATTA FWSGMAKQYE PHRINIIDTP GHVDFTIEVE RSMRVLDGAV MVYCAVGGVQ 120
PQSETVWRQA NKYKVPRIAF VNKMDRMGAN FLKVVGQIKT RLGANPVPLQ LAIGAEEGFT 180
GVVDLVKMKA INWNDADQGV TFEYEDIPAD MQDLANEWHQ NLIESAAEAS EELMEKYLGG 240
EELTEEEIKQ ALRQRVLNNE IILVTCGSAF KNKGVQAMLD AVIDYLPSPV DVPAINGILD 300
DGKDTPAERH ASDDEPFSAL AFKIATDPFV GNLTFFRVYS GVVNSGDTVL NSVKTARERF 360
GRIVQMHANK REEIKEVRAG DIAAAIGLKD VTTGDTLCDP ENPIILERME FPEPVISIAV 420
EPKTKADQEK MGLALGRLAK EDPSFRVWTD EESNQTIIAG MGELHLDIIV DRMKREFNVE 480
ANVGKPQVAY REAIRAKVTD IEGKHAKQSG GRGQYGHVVI DMYPLEPGSN PKGYEFINDI 540
KGGVIPGEYI PAVDKGIQEQ LKSGPLAGYP VVDLGVRLHF GSYHDVDSSE LAFKLAASIA 600
FKEGFKKAKP VLLEPIMKVE VETPEENTGD VIGDLSRRRG MLKGQESEVT GVKIHAEVPL 660
SEMFGYATQL RSLTKGRASY TMEFLKYDDA PNNVAQAVIE ARGK 704 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005525; F:GTP binding; IEA:HAMAP.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; IEA:HAMAP.
 GO:0006184; P:GTP catabolic process; IEA:GOC. 
Interpro
 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.
 IPR004540; Transl_elong_EFG/EF2.
 IPR005517; Transl_elong_EFG/EF2_IV.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00679; EFG_C
 PF03764; EFG_IV
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2 
SMART
 SM00838; EFG_C
 SM00889; EFG_IV 
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.