CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002864
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
 STM2583 
Created Date
 July 27, 2013 
Organism
 Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 
NCBI Taxa ID
 99287 
Lysine Modification
Position
Peptide
Type
References
164DAVRCSAKTGVGVTDacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
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 14 19 GTP (By similarity).
 NP_BIND 131 134 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
 599 AA 
Protein Sequence
MKNIRNFSII AHIDHGKSTL SDRIIQICGG LSDREMEAQV LDSMDLERER GITIKAQSVT 60
LDFKASDGET YQLNFIDTPG HVDFSYEVSR SLAACEGALL VVDAGQGVEA QTLANCYTAM 120
EMDLEVVPVL NKIDLPAADP ERVAEEIEDI VGIDATDAVR CSAKTGVGVT DVLERLVRDI 180
PPPQGDPDGP LQALIIDSWF DNYLGVVSLV RIKNGTMRKG DKIKVMSTGQ TYNADRLGIF 240
TPKQVDRTEL KCGEVGWLVC AIKDILGAPV GDTLTSARNP AEKALPGFKK VKPQVYAGLF 300
PVSSDDYESF RDALGKLSLN DASLFYEPES SSALGFGFRC GFLGLLHMEI IQERLEREYD 360
LDLITTAPTV VYEVETTAKE TIYVDSPSKL PPLNNIYELR EPIAECHMLL PQAYLGNVIT 420
LCIEKRGVQT NMVYHGNQVA LTYEIPMAEV VLDFFDRLKS TSRGYASLDY NFKRFQASDM 480
VRVDVLINNE RVDALALITH RDNSQSRGRE LVEKMKDLIP RQQFDIAIQA AIGTHIIARS 540
TVKQLRKNVL AKCYGGDISR KKKLLQKQKE GKKRMKQIGN VELPQEAFLA ILHVGKDNK 599 
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.