CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010152
UniProt Accession
Genbank Protein ID
 U00089 
Genbank Nucleotide ID
Protein Name
 Elongation factor G 
Protein Synonyms/Alias
 EF-G 
Gene Name
 fusA 
Gene Synonyms/Alias
 fus; MPN_227; MP604 
Created Date
 July 27, 2013 
Organism
 Mycoplasma pneumoniae (strain ATCC 29342 / M129) 
NCBI Taxa ID
 272634 
Lysine Modification
Position
Peptide
Type
References
136PRIIFVNKMDKTGANacetylation[1]
190VYFFDGGKEEKAEEKacetylation[1]
197KEEKAEEKPIPDQFKacetylation[1]
427KMSIALSKLAEEDPTacetylation[1]
486SFRETFNKESEVEGKacetylation[1]
493KESEVEGKYIKQSGGacetylation[1]
587IAASLALKEAGKVCSacetylation[1]
Reference
 [1] Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.
 van Noort V, Seebacher J, Bader S, Mohammed S, Vonkova I, Betts MJ, Kühner S, Kumar R, Maier T, O'Flaherty M, Rybin V, Schmeisky A, Yus E, Stülke J, Serrano L, Russell RB, Heck AJ, Bork P, Gavin AC.
 Mol Syst Biol. 2012 Feb 28;8:571. [PMID: 22373819] 
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; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 688 AA 
Protein Sequence
MARTVDLINF RNFGIMAHID AGKTTTSERI LFHSGRIHKI GETHDGESVM DWMEQEKERG 60
ITITSAATSV SWKNCSLNLI DTPGHVDFTV EVERSLRVLD GAIAVLDAQM GVEPQTETVW 120
RQASRYEVPR IIFVNKMDKT GANFERSVQS IQQRLGVKAV PIQLPIGAEN DFNGIIDLIE 180
EKVYFFDGGK EEKAEEKPIP DQFKDQVKQM RAHLVEEVAN FDDQLMADYL EGKEISIADI 240
KRCIRKGVIG CQFFPVLCGS AFKNKGIKLL LDAVVDFLPS PVDVPQAKAY GEDGNEVLIS 300
ASDDAPFVGL AFKVATDPFV GRLTFVRVYS GVLKSGSYVK NVRKNKKERV SRLVKMHAQN 360
RNEIEEIRAG DICAIIGLKD TTTGETLVDD KIDVQLEAMQ FAQPVISLAV EPKTKADQEK 420
MSIALSKLAE EDPTFKTFTD PETGQTIIAG MGELHLDILV DRMRREFKVE VNVGAPQVSF 480
RETFNKESEV EGKYIKQSGG RGQYGHVKIR FEPNKDKGFE FVDKIVGGRI PREYIKPVQA 540
GLENAMASGP LAGYPMIDIK ATLFDGSFHE VDSSEMAFKI AASLALKEAG KVCSPVLLEP 600
IMAIEVTVPE QYFGDTMGDI SSRRGLIEGT EQRDNVQVIK AKVPLKEMFG YATDLRSFSQ 660
GRGNYVMQFS HYAETPKSVV NEIIATKK 688 
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.