| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Elongation factor P |
Protein Synonyms/Alias | EF-P |
Gene Name | efp |
Gene Synonyms/Alias | b4147, JW4107 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | | 5 | ***MATYYSNDFRAG | Y | HTP | [1] | | 4 | ****MATYYSNDFRA | Y | HTP | [1] | |
Reference | [1]The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence. Hansen AM,Chaerkady R,Sharma J,Díaz-Mejía JJ,Tyagi N,Renuse S,Jacob HK,Pinto SM,Sahasrabuddhe NA,Kim MS,Delanghe B,Srinivasan N,Emili A,Kaper JB,Pandey A PLoS Pathog. 2013;9(6):e1003403. [ PMID:23785281] |
Functional Description From UniProt | FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Beta-lysylation at Lys-34 is required for alleviation. The Pro codons and their context do not affect activity; only consecutive Pro residues (not another amino acid) are affected by EF-P. Has stimulatory effects on peptide bond formation between ribosome-bound initiator tRNA(fMet) and puromycin, and N-acetyl-Phe tRNA(Phe)-primed poly(U)-directed poly(Phe) synthesis |
| MOD_RES 34 34 N6-(3,6-diaminohexanoyl)-5-hydroxylysine |
| 3D-structure; Completeproteome; Cytoplasm; Directproteinsequencing; Elongationfactor; Hydroxylation; Proteinbiosynthesis; Referenceproteome |
Protein Sequence | MATYYSNDFR AGLKIMLDGE PYAVEASEFV KPGKGQAFAR VKLRRLLTGT RVEKTFKSTD 60
SAEGADVVDM NLTYLYNDGE FWHFMNNETF EQLSADAKAI GDNAKWLLDQ AECIVTLWNG 120
QPISVTPPNF VELEIVDTDP GLKGDTAGTG GKPATLSTGA VVKVPLFVQI GEVIKVDTRS 180
GEYVSRVK 188 |
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