ID EPMA_SODGM Reviewed; 325 AA.
AC Q2NW90;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Elongation factor P--(R)-beta-lysine ligase {ECO:0000255|HAMAP-Rule:MF_00174};
DE Short=EF-P--(R)-beta-lysine ligase {ECO:0000255|HAMAP-Rule:MF_00174};
DE EC=6.3.1.- {ECO:0000255|HAMAP-Rule:MF_00174};
DE AltName: Full=EF-P post-translational modification enzyme A {ECO:0000255|HAMAP-Rule:MF_00174};
DE AltName: Full=EF-P-lysine lysyltransferase {ECO:0000255|HAMAP-Rule:MF_00174};
GN Name=epmA {ECO:0000255|HAMAP-Rule:MF_00174}; Synonyms=yjeA;
GN OrderedLocusNames=SG0310;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
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. {ECO:0000255|HAMAP-Rule:MF_00174}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00174}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC EpmA subfamily. {ECO:0000255|HAMAP-Rule:MF_00174}.
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DR EMBL; AP008232; BAE73585.1; -; Genomic_DNA.
DR RefSeq; WP_011410173.1; NZ_LN854557.1.
DR AlphaFoldDB; Q2NW90; -.
DR SMR; Q2NW90; -.
DR STRING; 343509.SG0310; -.
DR KEGG; sgl:SG0310; -.
DR eggNOG; COG2269; Bacteria.
DR HOGENOM; CLU_008255_1_1_6; -.
DR OrthoDB; 9802326at2; -.
DR BioCyc; SGLO343509:SGP1_RS02860-MONOMER; -.
DR Proteomes; UP000001932; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016880; F:acid-ammonia (or amide) ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR HAMAP; MF_00174; EF_P_modif_A; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004525; EpmA.
DR InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR NCBIfam; TIGR00462; genX; 1.
DR PANTHER; PTHR42918:SF6; ELONGATION FACTOR P--(R)-BETA-LYSINE LIGASE; 1.
DR PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding.
FT CHAIN 1..325
FT /note="Elongation factor P--(R)-beta-lysine ligase"
FT /id="PRO_1000023632"
FT BINDING 76..78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT BINDING 100..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT BINDING 244..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT BINDING 300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
SQ SEQUENCE 325 AA; 36453 MW; F2EF00900C4408B5 CRC64;
MSDSASWQPS APIANLLKRA AIVGQIRRFF SDRGLLEVET PAMSQATVTD IHLVPFQTCF
IGPGAAGGMP LYLMTSPEYH MKRLLAAGSG PLFQLCRSFR NEEAGRYHNP EFTMLEWYRP
HYDMYRLMNE VDDLLQQILD CDSAETLSYQ QVFTRHVGID PLSADKAQLY DAAVKWDLGE
AASVEDDRDT LLQLLFAMVV EPNIGHDKPA FVYHFPASQA ALAEISTEDH RVADRFEAYF
KGIELANGFC ELTDAREQRQ RFEQDNRKRV AMKLSEQPID ENLLAALAQG MPECSGVALG
VDRLVMLALK ADRLSDVIAF AVERA
//
