CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013739
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor G 
Protein Synonyms/Alias
 EF-G 
Gene Name
 fusA 
Gene Synonyms/Alias
 GK0103 
Created Date
 July 27, 2013 
Organism
 Geobacillus kaustophilus (strain HTA426) 
NCBI Taxa ID
 235909 
Lysine Modification
Position
Peptide
Type
References
139VFVNKMDKIGADFLYacetylation[1]
213MAEEYHNKLIEAVAEacetylation[1]
367NHRQEISKVYAGDIAacetylation[1]
414ISVAIEPKSKADQDKacetylation[1]
519FSPNERGKGFEFENAacetylation[1]
564PVVDIKAKLFDGSYHacetylation[1]
581DSSEMAFKIAASLALacetylation[1]
Reference
 [1] Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus.
 Lee DW, Kim D, Lee YJ, Kim JA, Choi JY, Kang S, Pan JG.
 Proteomics. 2013 Aug;13(15):2278-82. [PMID: 23696451] 
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 81 85 GTP (By similarity).
 NP_BIND 135 138 GTP (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding; Protein biosynthesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 692 AA 
Protein Sequence
MAREFSLEKT RNIGIMAHID AGKTTTTERI LFYTGRVHKI GEVHEGAATM DWMEQEQERG 60
ITITSAATTA QWKGHRINII DTPGHVDFTV EVERSLRVLD GAITVLDAQS GVEPQTETVW 120
RQATTYGVPR IVFVNKMDKI GADFLYSVKT LHDRLQANAH PVQLPIGAED QFSGIIDLVE 180
MCAYHYHDEL GKNIERIDIP EEYRDMAEEY HNKLIEAVAE LDEELMMKYL EGEEITTEEL 240
KAAIRKATIS VEFFPVFCGS AFKNKGVQLL LDGVVDYLPS PVDIPAIRGV VPDTEEEVTR 300
EASDDAPFAA LAFKIMTDPY VGKLTFIRVY SGTLDSGSYV MNTTKGKRER IGRLLQMHAN 360
HRQEISKVYA GDIAAAVGLK DTTTGDTLCD EKHPVILESM QFPEPVISVA IEPKSKADQD 420
KMSQALQKLQ EEDPTFRAHT DPETGQTIIS GMGELHLDII VDRMRREFKV EANVGAPQVA 480
YRETFRKSAQ VEGKFIRQSG GRGQYGHVWI EFSPNERGKG FEFENAIVGG VVPKEYVPAV 540
QAGLEEAMQN GVLAGYPVVD IKAKLFDGSY HDVDSSEMAF KIAASLALKN AATKCDPVLL 600
EPIMKVEVVI PEEYLGDIMG DITSRRGRIE GMEARGNAQV VRAMVPMAEM FGYATSLRSN 660
TQGRGTFSMV FDHYEEVPKN IADEIIKKNK GE 692 
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.