EPMA_PHOLL
ID EPMA_PHOLL Reviewed; 325 AA.
AC Q7MZY6;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=genX, yjeA;
GN OrderedLocusNames=plu4121;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571872; CAE16493.1; -; Genomic_DNA.
DR RefSeq; WP_011148239.1; NC_005126.1.
DR AlphaFoldDB; Q7MZY6; -.
DR SMR; Q7MZY6; -.
DR STRING; 243265.plu4121; -.
DR EnsemblBacteria; CAE16493; CAE16493; plu4121.
DR GeneID; 24168687; -.
DR KEGG; plu:plu4121; -.
DR eggNOG; COG2269; Bacteria.
DR HOGENOM; CLU_008255_1_1_6; -.
DR OMA; EWYRPGF; -.
DR OrthoDB; 63621at2; -.
DR BioCyc; PLUM243265:PLU_RS20385-MON; -.
DR Proteomes; UP000002514; 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 GO; GO:0071915; P:protein-lysine lysylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
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 Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00462; genX; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..325
FT /note="Elongation factor P--(R)-beta-lysine ligase"
FT /id="PRO_0000152726"
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; 36754 MW; 74BD358E10F54A61 CRC64;
MSETANWQPS AAIANLLKRA TILAEIRRFF ADRGVLEVET PAMGQFTVTD IQLFSFQTEF
VGPGAADGMT LYLMTSPEYH MKRLLAAGSG PIYQLGRCFR NEEAGRYHNP EFTMLEWYRP
HYDMYRLMNE VDDLLQQILD CESAESLSYQ QAFLRYLDID PLSAEKEKLR EIAAKLDLSN
IADIEEDRDT LLQLLFAVGV EPHIGTEKPT FIYHFPASQA SLAEISKEDH RVAERFEVYF
KGVELANGFR ELTDSHEQCQ RFERDNRKRA ALGLPVRPID ENLIGALKQG MPECAGVALG
VDRLVMLALG AEKLSDVMAF SITKA