CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013874
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor G 
Protein Synonyms/Alias
 EF-G 
Gene Name
 fusA 
Gene Synonyms/Alias
 fus; TTHA1695 
Created Date
 July 27, 2013 
Organism
 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) 
NCBI Taxa ID
 300852 
Lysine Modification
Position
Peptide
Type
References
4****MAVKVEYDLKRacetylation[1]
10VKVEYDLKRLRNIGIacetylation[1]
423KTKADQEKLSQALARacetylation[1]
Reference
 [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus.
 Okanishi H, Kim K, Masui R, Kuramitsu S.
 J Proteome Res. 2013 Aug 1;. [PMID: 23901841] 
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 19 26 GTP (By similarity).
 NP_BIND 83 87 GTP (By similarity).
 NP_BIND 137 140 GTP (By similarity).  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 691 AA 
Protein Sequence
MAVKVEYDLK RLRNIGIAAH IDAGKTTTTE RILYYTGRIH KIGEVHEGAA TMDFMEQERE 60
RGITITAAVT TCFWKDHRIN IIDTPGHVDF TIEVERSMRV LDGAIVVFDS SQGVEPQSET 120
VWRQAEKYKV PRIAFANKMD KTGADLWLVI RTMQERLGAR PVVMQLPIGR EDTFSGIIDV 180
LRMKAYTYGN DLGTDIREIP IPEEYLDQAR EYHEKLVEVA ADFDENIMLK YLEGEEPTEE 240
ELVAAIRKGT IDLKITPVFL GSALKNKGVQ LLLDAVVDYL PSPLDIPPIK GTTPEGEVVE 300
IHPDPNGPLA ALAFKIMADP YVGRLTFIRV YSGTLTSGSY VYNTTKGRKE RVARLLRMHA 360
NHREEVEELK AGDLGAVVGL KETITGDTLV GEDAPRVILE SIEVPEPVID VAIEPKTKAD 420
QEKLSQALAR LAEEDPTFRV STHPETGQTI ISGMGELHLE IIVDRLKREF KVDANVGKPQ 480
VAYRETITKP VDVEGKFIRQ TGGRGQYGHV KIKVEPLPRG SGFEFVNAIV GGVIPKEYIP 540
AVQKGIEEAM QSGPLIGFPV VDIKVTLYDG SYHEVDSSEM AFKIAGSMAI KEAVQKGDPV 600
ILEPIMRVEV TTPEEYMGDV IGDLNARRGQ ILGMEPRGNA QVIRAFVPLA EMFGYATDLR 660
SKTQGRGSFV MFFDHYQEVP KQVQEKLIKG Q 691 
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.