CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010481
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor G 
Protein Synonyms/Alias
 EF-G; Vegetative protein 19; VEG19 
Gene Name
 fusA 
Gene Synonyms/Alias
 fus; BSU01120 
Created Date
 July 27, 2013 
Organism
 Bacillus subtilis (strain 168) 
NCBI Taxa ID
 224308 
Lysine Modification
Position
Peptide
Type
References
9AREFSLEKTRNIGIMacetylation[1]
341LDSGSYVKNSTKGKRacetylation[1]
494TGAKVEGKFVRQSGGacetylation[1]
Reference
 [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis.
 Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG.
 Proteomics. 2013 May;13(10-11):1726-36. [PMID: 23468065] 
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).
 MOD_RES 213 213 Phosphoserine.
 MOD_RES 302 302 Phosphoserine.
 MOD_RES 569 569 Phosphoserine.
 MOD_RES 680 680 Phosphoserine.  
Keyword
 Complete proteome; Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 692 AA 
Protein Sequence
MAREFSLEKT RNIGIMAHID AGKTTTTERI LFYTGRIHKI GETHEGASQM DWMEQEQERG 60
ITITSAATTA QWKGYRVNII DTPGHVDFTV EVERSLRVLD GAVAVLDAQS GVEPQTETVW 120
RQATTYGVPR IVFVNKMDKI GADFLYSVGT LRDRLQANAH AIQLPIGAED NFEGIIDLVE 180
NVAYFYEDDL GTRSDAKEIP EEYKEQAEEL RNSLIEAVCE LDEELMDKYL EGEEITIDEL 240
KAGIRKGTLN VEFYPVLVGS AFKNKGVQLV LDAVLDYLPA PTDVAAIKGT RPDTNEEIER 300
HSSDEEPFSA LAFKVMTDPY VGKLTFFRVY SGTLDSGSYV KNSTKGKRER VGRILQMHAN 360
SREEISTVYA GDIAAAVGLK DTTTGDTLCD EKDLVILESM EFPEPVIDVA IEPKSKADQD 420
KMGIALAKLA EEDPTFRTQT NPETGQTIIS GMGELHLDII VDRMKREFKV EANVGAPQVA 480
YRETFRTGAK VEGKFVRQSG GRGQFGHVWI EFEPNEEGAG FEFENAIVGG VVPREYIPAV 540
QAGLEDALEN GVLAGFPLID IKAKLFDGSY HDVDSNEMAF KVAASMALKN AVSKCNPVLL 600
EPIMKVEVVI PEEYMGDIMG DITSRRGRVE GMEARGNAQV VRAMVPLAEM FGYATALRSN 660
TQGRGTFTMH MDHYEEVPKS VAEEIIKKNK 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.