CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002926
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor G 
Protein Synonyms/Alias
 EF-G 
Gene Name
 fusA 
Gene Synonyms/Alias
 far; fus; b3340; JW3302 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
39FYTGVNHKIGEVHDGacetylation[1]
77AFWSGMAKQYEPHRIacetylation[1]
143PRIAFVNKMDRMGANacetylation[1, 2, 3]
153RMGANFLKVVNQIKTacetylation[1, 2]
159LKVVNQIKTRLGANPacetylation[1, 3]
187TGVVDLVKMKAINWNacetylation[1]
249ELTEAEIKGALRQRVacetylation[1]
354DTVLNSVKAARERFGacetylation[1]
370IVQMHANKREEIKEVacetylation[1, 3]
375ANKREEIKEVRAGDIacetylation[1, 3]
389IAAAIGLKDVTTGDTacetylation[1]
423ISIAVEPKTKADQEKacetylation[1, 3]
425IAVEPKTKADQEKMGacetylation[1]
430KTKADQEKMGLALGRacetylation[1]
440LALGRLAKEDPSFRVacetylation[1]
485NVEANVGKPQVAYREacetylation[1, 3]
497YRETIRQKVTDVEGKacetylation[1]
504KVTDVEGKHAKQSGGacetylation[1, 3, 4]
507DVEGKHAKQSGGRGQacetylation[1]
532LEPGSNPKGYEFINDacetylation[1, 3]
541YEFINDIKGGVIPGEacetylation[1]
555EYIPAVDKGIQEQLKacetylation[1, 2, 3]
562KGIQEQLKAGPLAGYacetylation[1, 3]
602LAASIAFKEGFKKAKacetylation[1, 3]
606IAFKEGFKKAKPVLLacetylation[1]
607AFKEGFKKAKPVLLEacetylation[1]
609KEGFKKAKPVLLEPIacetylation[1, 3]
618VLLEPIMKVEVETPEacetylation[1, 3]
643SRRRGMLKGQESEVTacetylation[1, 3, 4]
675TQLRSLTKGRASYTMacetylation[3]
686SYTMEFLKYDEAPSNacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [3] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [4] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842] 
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. 
Sequence Annotation
 NP_BIND 17 24 GTP (By similarity).
 NP_BIND 88 92 GTP (By similarity).
 NP_BIND 142 145 GTP (By similarity).
 MOD_RES 504 504 N6-acetyllysine.
 MOD_RES 643 643 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; 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 FLKVVNQIKT RLGANPVPLQ LAIGAEEHFT 180
GVVDLVKMKA INWNDADQGV TFEYEDIPAD MVELANEWHQ NLIESAAEAS EELMEKYLGG 240
EELTEAEIKG ALRQRVLNNE IILVTCGSAF KNKGVQAMLD AVIDYLPSPV DVPAINGILD 300
DGKDTPAERH ASDDEPFSAL AFKIATDPFV GNLTFFRVYS GVVNSGDTVL NSVKAARERF 360
GRIVQMHANK REEIKEVRAG DIAAAIGLKD VTTGDTLCDP DAPIILERME FPEPVISIAV 420
EPKTKADQEK MGLALGRLAK EDPSFRVWTD EESNQTIIAG MGELHLDIIV DRMKREFNVE 480
ANVGKPQVAY RETIRQKVTD VEGKHAKQSG GRGQYGHVVI DMYPLEPGSN PKGYEFINDI 540
KGGVIPGEYI PAVDKGIQEQ LKAGPLAGYP VVDMGIRLHF GSYHDVDSSE LAFKLAASIA 600
FKEGFKKAKP VLLEPIMKVE VETPEENTGD VIGDLSRRRG MLKGQESEVT GVKIHAEVPL 660
SEMFGYATQL RSLTKGRASY TMEFLKYDEA PSNVAQAVIE ARGK 704 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 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.