RegulonDB RegulonDB 11.1: Gene Form
   

efp gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

epmB efp ecnA ppGpp anti-anti-terminator anti-terminator terminator terminator TSS_4965 (cluster) TSS_4965 (cluster) epmBp3 epmBp3 TSS_4964 TSS_4964 TSS_4963 TSS_4963 TSS_4962 TSS_4962 TSS_4961 TSS_4961 efpp efpp

Gene      
Name: efp    Texpresso search in the literature
Synonym(s): ECK4141, EG12099, b4147
Genome position(nucleotides): 4375699 --> 4376265
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 49.38
External database links:  
ASAP:
 ABE-0013583
CGSC:
 34470
ECHOBASE:
 EB2023
ECOLIHUB:
 efp
OU-MICROARRAY:
 b4147
STRING:
 511145.b4147
COLOMBOS: efp


Product      
Name: protein chain elongation factor EF-P
Synonym(s): EF-P, Efp
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 20.591
Isoelectric point: 4.635
Motif(s):
 
Type Positions Sequence Comment
2 -> 188 ATYYSNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVVDMNLTYLYNDGEFWHFMNNETFEQLSADAKAIGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEIVDTDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSRVK UniProt: Elongation factor P.
7 -> 61 NDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDS
31 -> 31 K UniProt: No lysylation..
33 -> 33 G UniProt: No lysylation. Loss of in vivo EF-P function for cell growth..
34 -> 34 K UniProt: No lysylation and loss of EF-P activity. No facilitation of translation of poly-Pro stretches..

 
Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.2 - translation
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0003746 - translation elongation factor activity
GO:0043022 - ribosome binding
biological_process GO:2001125 - negative regulation of translational frameshifting
GO:0006412 - translation
GO:0006414 - translational elongation
GO:0043043 - peptide biosynthetic process
GO:0072344 - rescue of stalled ribosome
Note(s): Note(s): ...[more].
Evidence: [EXP-IDA-PURIFIED-PROTEIN] Assay of protein purified to homogeneity
Reference(s): [1] Aoki H., et al., 1991
[2] Glick BR., et al., 1976
[3] Mandal A., et al., 2014
[4] Sumida T., et al., 2010
External database links:  
ALPHAFOLD:
 P0A6N4
DIP:
 DIP-31834N
ECOCYC:
 EG12099-MONOMER
ECOLIWIKI:
 b4147
INTERPRO:
 IPR001059
INTERPRO:
 IPR012340
INTERPRO:
 IPR011768
INTERPRO:
 IPR008991
INTERPRO:
 IPR013852
INTERPRO:
 IPR014722
INTERPRO:
 IPR015365
INTERPRO:
 IPR020599
INTERPRO:
 IPR013185
PANTHER:
 PTHR30053
PDB:
 6ENU
PDB:
 3A5Z
PDB:
 6ENJ
PFAM:
 PF08207
PFAM:
 PF01132
PFAM:
 PF09285
PRIDE:
 P0A6N4
PRODB:
 PRO_000022504
PROSITE:
 PS01275
REFSEQ:
 NP_418571
SMART:
 SM00841
SMART:
 SM01185
SMR:
 P0A6N4
SWISSMODEL:
 P0A6N4
UNIPROT:
 P0A6N4


Operon      
Name: efp         
Operon arrangement:
Transcription unit        Promoter
efp


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_4961 4375628 reverse nd [RS-EPT-CBR] [5]
  promoter TSS_4962 4375655 forward nd [RS-EPT-CBR] [5]
  promoter TSS_4963 4375684 forward nd [RS-EPT-CBR] [5]
  promoter TSS_4964 4375700 reverse nd [RS-EPT-CBR] [5]
  promoter epmBp3 4375703 reverse nd [COMP-AINF] [6]
  promoter TSS_4965 (cluster) 4375964 forward nd [RS-EPT-CBR] [5]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

 [COMP-AINF] Inferred computationally without human oversight


Reference(s)    

 [1] Aoki H., Adams SL., Chung DG., Yaguchi M., Chuang SE., Ganoza MC., 1991, Cloning, sequencing and overexpression of the gene for prokaryotic factor EF-P involved in peptide bond synthesis., Nucleic Acids Res 19(22):6215-20

 [2] Glick BR., Ganoza MC., 1976, Characterization and site of action of a soluble protein that stimulates peptide-bond synthesis., Eur J Biochem 71(2):483-91

 [3] Mandal A., Mandal S., Park MH., 2014, Genome-wide analyses and functional classification of proline repeat-rich proteins: potential role of eIF5A in eukaryotic evolution., PLoS One 9(11):e111800

 [4] Sumida T., Yanagisawa T., Ishii R., Yokoyama S., 2010, Crystallization and preliminary X-ray crystallographic study of GenX, a lysyl-tRNA synthetase paralogue from Escherichia coli, in complex with translation elongation factor P., Acta Crystallogr Sect F Struct Biol Cryst Commun 66(Pt 9):1115-8

 [5] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

 [6] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

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