ID   EPMA_HISS2              Reviewed;         323 AA.
AC   B0USM2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 93.
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=6.3.2.- {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=HSM_0783;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-beta-lysine + L-lysyl-[protein] + ATP = N(6)-((3R)-3,6-
CC         diaminohexanoyl)-L-lysyl-[protein] + AMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:83435, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:20131,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:84138, ChEBI:CHEBI:156053,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000255|HAMAP-Rule:MF_00174};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83436;
CC         Evidence={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; CP000947; ACA32455.1; -; Genomic_DNA.
DR   RefSeq; WP_011609430.1; NC_010519.1.
DR   AlphaFoldDB; B0USM2; -.
DR   SMR; B0USM2; -.
DR   STRING; 228400.HSM_0783; -.
DR   GeneID; 31487072; -.
DR   KEGG; hsm:HSM_0783; -.
DR   HOGENOM; CLU_008255_1_1_6; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0052868; F:protein-lysine lysyltransferase activity; IEA:RHEA.
DR   GO; GO:0000049; F:tRNA binding; IEA:TreeGrafter.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR   FunFam; 3.30.930.10:FF:000017; Elongation factor P--(R)-beta-lysine ligase; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 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   NCBIfam; TIGR00462; genX; 1.
DR   NCBIfam; NF006828; PRK09350.1; 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..323
FT                   /note="Elongation factor P--(R)-beta-lysine ligase"
FT                   /id="PRO_1000077139"
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         242..243
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
FT   BINDING         298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00174"
SQ   SEQUENCE   323 AA;  36724 MW;  891B7D8848B20F22 CRC64;
     MSLNEQWQPS ASIQNLLARA KIIADIRRFF TERGLLEVET PVLSEFGVTD VHLSTFSTAF
     TSPFMEKSKT LWLTTSPEYH MKRLLAAGSG AIFQLCKVFR NEESGKKHNP EFTMLEWYRP
     HFDMHRLINE VDDLLQQTLD CEPAEMASYQ FVFQEHVGID PLSAPINELI EKARECHLDG
     AENEDRDTLL QFLFSTLVEP NIGQNKPIAV YHFPATQAAL AQISSEDHRV AERFEFYYKG
     IELANGFNEL TDAQEQEHRF NQDNRLREQL GLPQHEIDHR FLGALQAGLP NTAGVALGVD
     RLIMLALGAE NISEVISFNI DCA
//