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Annotation rule MF_00174
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General rule information [?]

Accession MF_00174
Dates 1-JUN-2001 (Created)
18-NOV-2019 (Last updated, Version 23)
Name EF_P_modif_A
Scope
Bacteria; Gammaproteobacteria
Templates P0A8N7 (EPMA_ECOLI); Q9ZJ12 (EPMA_SALTY): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
EPMA
Protein name
RecName: Full=Elongation factor P--(R)-beta-lysine ligase;
Short=EF-P--(R)-beta-lysine ligase;
EC 6.3.1.-;
AltName: Full=EF-P-lysine lysyltransferase;
AltName: Full=EF-P post-translational modification enzyme A;
Gene name
epmA

Comments [?]

case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
Function With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.
else
Function With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.
end case
Subunit Homodimer.
Similarity Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

Keywords [?]


Gene Ontology [?]

GO:0005524; Molecular function: ATP binding.
GO:0016880; Molecular function: acid-ammonia (or amide) ligase activity.
GO:0071915; Biological process: protein-lysine lysylation.

Cross-references [?]

Pfam PF00152; tRNA-synt_2; 1;
PRINTS PR00982; TRNASYNTHLYS; 1;
TIGRFAMs TIGR00462; GenX; 1;
PROSITE PS50862; AA_TRNA_LIGASE_II; 1;

Features [?]

From: EPMA_ECOLI (P0A8N7)
Key     From     To       Description   Tag   Condition   FTGroup
NP_BIND     100     102       ATP     R-x-[EQKN]  
NP_BIND     244     245       ATP     E-L  
REGION     76     78       Substrate binding     S-x-E  
BINDING     109     109       ATP; via amide nitrogen and carbonyl oxygen     N  
BINDING     118     118       Substrate     Y  
BINDING     251     251       Substrate     E  
BINDING     300     300       ATP; via amide nitrogen     G  

Additional information [?]

Size range 293-327 amino acids
Related rules None
Fusion None