CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009247
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
 b2569; JW2553 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
224LRKGDKVKVMSTGQTacetylation[1]
243RLGIFTPKQVDRTELacetylation[2]
283LARNPAEKALPGFKKacetylation[2]
289EKALPGFKKVKPQVYacetylation[2]
473ASLDYNFKRFQASDMacetylation[2]
514RGRELVEKMKDLIPRacetylation[2]
516RELVEKMKDLIPRQQacetylation[2]
Reference
 [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [2] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 
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. 
Sequence Annotation
 NP_BIND 14 19 GTP (By similarity).
 NP_BIND 131 134 GTP (By similarity).  
Keyword
 3D-structure; 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
 599 AA 
Protein Sequence
MKNIRNFSII AHIDHGKSTL SDRIIQICGG LSDREMEAQV LDSMDLERER GITIKAQSVT 60
LDYKASDGET YQLNFIDTPG HVDFSYEVSR SLAACEGALL VVDAGQGVEA QTLANCYTAM 120
EMDLEVVPVL NKIDLPAADP ERVAEEIEDI VGIDATDAVR CSAKTGVGVQ DVLERLVRDI 180
PPPEGDPEGP LQALIIDSWF DNYLGVVSLI RIKNGTLRKG DKVKVMSTGQ TYNADRLGIF 240
TPKQVDRTEL KCGEVGWLVC AIKDIHGAPV GDTLTLARNP AEKALPGFKK VKPQVYAGLF 300
PVSSDDYEAF RDALGKLSLN DASLFYEPES SSALGFGFRC GFLGLLHMEI IQERLEREYD 360
LDLITTAPTV VYEVETTSRE VIYVDSPSKL PAVNNIYELR EPIAECHMLL PQAYLGNVIT 420
LCVEKRGVQT NMVYHGNQVA LTYEIPMAEV VLDFFDRLKS TSRGYASLDY NFKRFQASDM 480
VRVDVLINGE RVDALALITH RDNSQNRGRE LVEKMKDLIP RQQFDIAIQA AIGTHIIARS 540
TVKQLRKNVL AKCYGGDISR KKKLLQKQKE GKKRMKQIGN VELPQEAFLA ILHVGKDNK 599 
Gene Ontology
 GO:0005829; C:cytosol; IDA:EcoCyc.
 GO:0005886; C:plasma membrane; IDA:EcoCyc.
 GO:0005525; F:GTP binding; IEA:HAMAP.
 GO:0003924; F:GTPase activity; IDA:EcoCyc.
 GO:0043022; F:ribosome binding; IEA:HAMAP.
 GO:0003746; F:translation elongation factor activity; IDA:EcoCyc.
 GO:0045727; P:positive regulation of translation; IEA:HAMAP.
 GO:0009409; P:response to cold; IMP:EcoCyc.
 GO:0009268; P:response to pH; IMP:EcoCyc.
 GO:0009651; P:response to salt stress; IMP:EcoCyc. 
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.