CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002884
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor G 
Protein Synonyms/Alias
 EF-G 
Gene Name
 fusA 
Gene Synonyms/Alias
 Rv0684; MT0712; MTCY210.01; MTV040.12 
Created Date
 July 27, 2013 
Organism
 Mycobacterium tuberculosis 
NCBI Taxa ID
 1773 
Lysine Modification
Position
Peptide
Type
References
307EDEEVVRKATTDEPFpupylation[1]
Reference
 [1] Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis [corrected] .
 Festa RA, McAllister F, Pearce MJ, Mintseris J, Burns KE, Gygi SP, Darwin KH.
 PLoS One. 2010 Jan 6;5(1):e8589. [PMID: 20066036] 
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 20 27 GTP (By similarity).
 NP_BIND 84 88 GTP (By similarity).
 NP_BIND 138 141 GTP (By similarity).
 CROSSLNK 307 307 Isoglutamyl lysine isopeptide (Lys-Gln)  
Keyword
 Complete proteome; Cytoplasm; Elongation factor; GTP-binding; Isopeptide bond; Nucleotide-binding; Protein biosynthesis; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 701 AA 
Protein Sequence
MAQKDVLTDL SRVRNFGIMA HIDAGKTTTT ERILYYTGIN YKIGEVHDGA ATMDWMEQEQ 60
ERGITITSAA TTTFWKDNQL NIIDTPGHVD FTVEVERNLR VLDGAVAVFD GKEGVEPQSE 120
QVWRQADKYD VPRICFVNKM DKIGADFYFS VRTMGERLGA NAVPIQLPVG AEADFEGVVD 180
LVEMNAKVWR GETKLGETYD TVEIPADLAE QAEEYRTKLL EVVAESDEHL LEKYLGGEEL 240
TVDEIKGAIR KLTIASEIYP VLCGSAFKNK GVQPMLDAVV DYLPSPLDVP PAIGHAPAKE 300
DEEVVRKATT DEPFAALAFK IATHPFFGKL TYIRVYSGTV ESGSQVINAT KGKKERLGKL 360
FQMHSNKENP VDRASAGHIY AVIGLKDTTT GDTLSDPNQQ IVLESMTFPD PVIEVAIEPK 420
TKSDQEKLSL SIQKLAEEDP TFKVHLDSET GQTVIGGMGE LHLDILVDRM RREFKVEANV 480
GKPQVAYKET IKRLVQNVEY THKKQTGGSG QFAKVIINLE PFTGEEGATY EFESKVTGGR 540
IPREYIPSVD AGAQDAMQYG VLAGYPLVNL KVTLLDGAYH EVDSSEMAFK IAGSQVLKKA 600
AALAQPVILE PIMAVEVTTP EDYMGDVIGD LNSRRGQIQA MEERAGARVV RAHVPLSEMF 660
GYVGDLRSKT QGRANYSMVF DSYSEVPANV SKEIIAKATG E 701 
Gene Ontology
 GO:0005618; C:cell wall; IDA:MTBBASE.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:MTBBASE.
 GO:0005525; F:GTP binding; IEA:HAMAP.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; IEA:HAMAP.
 GO:0040007; P:growth; IMP:MTBBASE.
 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.