CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016925
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor 4 
Protein Synonyms/Alias
 EF-4; Ribosomal back-translocase LepA 
Gene Name
 lepA 
Gene Synonyms/Alias
 LA_1888 
Created Date
 July 27, 2013 
Organism
 Leptospira interrogans serogroup Icterohaemorrhagiae serovar La 
NCBI Taxa ID
 189518 
Lysine Modification
Position
Peptide
Type
References
375ITTAPSVKYIIRSKNmethylation[1]
Reference
 [1] High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans.
 Cao XJ, Dai J, Xu H, Nie S, Chang X, Hu BY, Sheng QH, Wang LS, Ning ZB, Li YX, Guo XK, Zhao GP, Zeng R.
 Cell Res. 2010 Feb;20(2):197-210. [PMID: 19918266
Functional Description
 Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner (By similarity). 
Sequence Annotation
 NP_BIND 18 23 GTP (By similarity).
 NP_BIND 135 138 GTP (By similarity).  
Keyword
 Cell inner membrane; Cell membrane; Complete proteome; GTP-binding; Hydrolase; Membrane; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 600 AA 
Protein Sequence
MSDKQQFIRN FSIIAHIDHG KSTLADRLLE IGQVTNDRTK KDQILDSMDI ERERGITIKA 60
NNATFDYLAE DGNTYIMNLL DTPGHVDFTY EVSRSLKACE GVLLIVDASQ GVEAQTLANL 120
YLAMEQDLEI LPVMNKIDLP AADVEKTKIQ IEESLGLDPQ KAVAISAKTG LNVKEVLEQI 180
TKQIPSPKGN SNAPLKALVY DSYFDPYMGV VIKIRIFDGR IKKGDRILMM STGKDFTVNE 240
VGINRINLTP KESLETGEVG YIIAGIKKVS DAKTGDTVTL FSNPTKESVP GYKEAKPMVF 300
AGLFPINGEQ FDELVDAIEK LKLNDAALVF EKESSIALGF GFRVGYLGLL HMEIVQERLE 360
REFNLDLITT APSVKYIIRS KNGEVEEIDN PSRFPEPITI ESTEEPYVKA TVITPNEYVG 420
NIMSLAMDKR GIQLDTVYLT QDKVQLTYEI PLAELIFEFY DKLKSFTRGY ASLDYEPSGY 480
KASQLVKMDI LVNGEPVDAL SMIVHRSKAE QRGREIIEKL KDLIPRHQFM IPLQAAVGGK 540
ILARESISAL RKNVTAKCYG GDITRKKKLL EKQKEGKKRM KQIGNVEIPQ EAFLAVLKTS 600 
Gene Ontology
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005525; F:GTP binding; IEA:HAMAP.
 GO:0003924; F:GTPase activity; IEA:HAMAP.
 GO:0043022; F:ribosome binding; IEA:HAMAP.
 GO:0003746; F:translation elongation factor activity; IEA:HAMAP.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0045727; P:positive regulation of translation; IEA:HAMAP.
 GO:0006414; P:translational elongation; IEA:GOC. 
Interpro
 IPR006297; EF-4.
 IPR000795; EF_GTP-bd_dom.
 IPR009022; EFG_III-V.
 IPR000640; EFG_V.
 IPR013842; LepA_GTP-bd_C.
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00679; EFG_C
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF06421; LepA_C 
SMART
 SM00838; EFG_C 
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.