AC   MF_00174;
DC   Protein; auto
TR   HAMAP; MF_00174; -; 1; level=0
XX
Names: EF_P_modif_A
XX
ID   EPMA
DE   RecName: Full=Elongation factor P--(R)-beta-lysine ligase;
DE            Short=EF-P--(R)-beta-lysine ligase;
DE            EC=6.3.1.-;
DE   AltName: Full=EF-P-lysine lysyltransferase;
DE   AltName: Full=EF-P post-translational modification enzyme A;
GN   Name=epmA;
XX
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
CC   -!- FUNCTION: With EpmB is involved in the beta-lysylation step of the
CC       post-translational modification of translation elongation factor P (EF-
CC       P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-
CC       lysine produced by EpmB, forming a lysyl-adenylate, from which the
CC       beta-lysyl moiety is then transferred to the epsilon-amino group of EF-
CC       P 'Lys-34'.
else
CC   -!- FUNCTION: With EpmB is involved in the beta-lysylation step of the
CC       post-translational modification of translation elongation factor P (EF-
CC       P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced
CC       by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is
CC       then transferred to the epsilon-amino group of a conserved specific
CC       lysine residue in EF-P.
end case
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       EpmA subfamily.
XX
DR   Pfam; PF00152; tRNA-synt_2; 1; trigger=no
DR   PRINTS; PR00982; TRNASYNTHLYS; 1; trigger=no
DR   NCBIfam; TIGR00462; GenX; 1; trigger=no
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no
XX
KW   ATP-binding
KW   Ligase
KW   Nucleotide-binding
XX
GO   GO:0005524; F:ATP binding
GO   GO:0016880; F:acid-ammonia (or amide) ligase activity
GO   GO:0071915; P:protein-lysine lysylation
XX
FT   From: EPMA_ECOLI (P0A8N7)
FT   BINDING         100..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R-x-[EQKN]
FT   BINDING         244..245
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: E-L
FT   BINDING         76..78
FT                   /ligand="substrate"
FT   Condition: S-x-E
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: N
FT   BINDING         118
FT                   /ligand="substrate"
FT   Condition: Y
FT   BINDING         251
FT                   /ligand="substrate"
FT   Condition: E
FT   BINDING         300
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
XX
Size: 293-327;
Related: None;
Template: P0A8N7; Q9ZJ12;
Scope:
 Bacteria; Gammaproteobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.27 2023/06/01
//