EPMA_PECAS
ID EPMA_PECAS Reviewed; 325 AA.
AC Q6D033;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=ECA3968;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX950851; CAG76865.1; -; Genomic_DNA.
DR RefSeq; WP_011095462.1; NC_004547.2.
DR AlphaFoldDB; Q6D033; -.
DR SMR; Q6D033; -.
DR STRING; 218491.ECA3968; -.
DR PRIDE; Q6D033; -.
DR EnsemblBacteria; CAG76865; CAG76865; ECA3968.
DR GeneID; 57210581; -.
DR KEGG; eca:ECA3968; -.
DR PATRIC; fig|218491.5.peg.4032; -.
DR eggNOG; COG2269; Bacteria.
DR HOGENOM; CLU_008255_1_1_6; -.
DR OMA; EWYRPGF; -.
DR OrthoDB; 63621at2; -.
DR Proteomes; UP000007966; 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_1000023622"
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; 36782 MW; 92734F2880F806D0 CRC64;
MSETTSWQPS ASVANLLKRA SIVAAVRRFF TDRGVLEVET PAMSQATVTD VFLYPFQTRF
VGPGAADGMT LYLMTSPEYH MKRLLAAGSG PIFQLCRSFR NEESGRHHNP EFTMLEWYRP
HYDMYRLMNE VDDLLQQVLD CESAEMLSYQ QAFLRHLEID PLSVDKAQLR EAAEKLGLGD
IACREDDRDS LVQMLFTFGV EPNIGRDKPA FVYHFPATQA SLAEISSEDH RVAERFEVYF
KGIELANGFR ELTDADEQRQ RFEQDNRKRA ARGLSQQPID ENLLAALKNG LPECSGVALG
VDRLIMLALK AEKLSDVIAF SVERA
