CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-035882
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor G 
Protein Synonyms/Alias
 EF-G 
Gene Name
 fusA 
Gene Synonyms/Alias
 EAM_3201 
Created Date
 July 27, 2013 
Organism
 Erwinia amylovora (strain ATCC 49946 / CCPPB 0273 / Ea273 / 27-3) 
NCBI Taxa ID
 716540 
Lysine Modification
Position
Peptide
Type
References
143PRIAFVNKMDRMGANacetylation[1]
Reference
 [1] Differential lysine acetylation profiles of Erwinia amylovora strains revealed by proteomics.
 Wu X, Vellaichamy A, Wang D, Zamdborg L, Kelleher NL, Huber SC, Zhao Y.
 J Proteomics. 2013 Feb 21;79:60-71. [PMID: 23234799] 
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. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 702 AA 
Protein Sequence
MARTTPITRY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMAQEQERG 60
ITITSAATTA FWSGMAKQFE PHRVNIIDTP GHVDFTIEVE RSMRVLDGAV MVYCAVGGVQ 120
PQSETVWRQA NKYKVPRIAF VNKMDRMGAN FLKVVSQIKS RLAANPVPIQ LAIGAEEKFT 180
GVVDLVKMKA INWNDADQGV TFEYEEIPAD MQELAEEWHQ NLVESAAEAS EELMEKYLGG 240
EELTEEEIKS ALRQRVLNNE VILVTCGSAF KNKGVQAMLD AVVEYLPAPT DVTAINGILD 300
DGKDTPAVRH SDDKEPFAAL AFKIATDPFV GNLTFFRVYS GVVNSGDTVM NPVKSQRERL 360
GRIVQMHANK REEIKEVRAG DIAAAIGLKD VTTGDTLCDP SNVIILERME FPEPVISVAV 420
EPKTKADQEK MGLALGRLAK EDPSFRVWTD EESGQTIIAG MGELHLDILV DRMKREFNVE 480
ANVGKPQVAY RETIRETVKD VEGKHAKQSG GRGQFGHVVI DMGPLEAGGP GYEFVNDIVG 540
GSIPKEFIPA VDKGIQEQLK SGPLAGYPVV DIKVRLHYGS YHDVDSSELA FKLAASLAFK 600
SAFGKAKPVL LEPVMKVEVE TPEDYMGDVI GDLNRRRGMI EGMEDTSTGK TVRAQVPLSE 660
MFGYATDLRS QTQGRASYSM EFLKYAEAPN NVAQAVIEAR GK 702 
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.