ID E5YJN3_9ENTR Unreviewed; 325 AA.
AC E5YJN3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Elongation factor P--(R)-beta-lysine ligase {ECO:0000256|HAMAP-Rule:MF_00174};
DE Short=EF-P--(R)-beta-lysine ligase {ECO:0000256|HAMAP-Rule:MF_00174};
DE EC=6.3.1.- {ECO:0000256|HAMAP-Rule:MF_00174};
DE AltName: Full=EF-P post-translational modification enzyme A {ECO:0000256|HAMAP-Rule:MF_00174};
DE AltName: Full=EF-P-lysine lysyltransferase {ECO:0000256|HAMAP-Rule:MF_00174};
GN Name=epmA {ECO:0000256|HAMAP-Rule:MF_00174};
GN ORFNames=HMPREF0864_02744 {ECO:0000313|EMBL:EFV39839.1};
OS Enterobacteriaceae bacterium 9_2_54FAA.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=469613 {ECO:0000313|EMBL:EFV39839.1, ECO:0000313|Proteomes:UP000004908};
RN [1] {ECO:0000313|EMBL:EFV39839.1, ECO:0000313|Proteomes:UP000004908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9_2_54FAA {ECO:0000313|EMBL:EFV39839.1,
RC ECO:0000313|Proteomes:UP000004908};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA Allen-Vercoe E., Ambrose C., Strauss J., Sibley C., Haas B., Nusbaum C.,
RA Birren B.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFV39839.1, ECO:0000313|Proteomes:UP000004908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9_2_54FAA {ECO:0000313|EMBL:EFV39839.1,
RC ECO:0000313|Proteomes:UP000004908};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., Ambrose C.,
RA Strauss J., Sibley C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterobacteriaceae bacterium 9_2_54FAA.";
RL Submitted (MAR-2013) 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:0000256|HAMAP-Rule:MF_00174}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00174}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC EpmA subfamily. {ECO:0000256|HAMAP-Rule:MF_00174}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFV39839.1}.
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DR EMBL; ADCU02000001; EFV39839.1; -; Genomic_DNA.
DR AlphaFoldDB; E5YJN3; -.
DR Proteomes; UP000004908; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_00174};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00174, ECO:0000313|EMBL:EFV39839.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00174}.
FT DOMAIN 22..321
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 76..78
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00174"
FT BINDING 100..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00174"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00174"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00174"
FT BINDING 244..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00174"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00174"
FT BINDING 300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00174"
SQ SEQUENCE 325 AA; 36835 MW; D4FEDC3B56B21A76 CRC64;
MSETASWQPS APIANLLKRA TIMSTIRRFF SDRGVLEVDT PAMSQATVTD IHLVPFQTHF
VGPGAAQGMT LYMMTSPEYH MKRLLAAGSG PIYQLGKSFR NEESGRHHNP EFSMLEWYRP
HYDMYRLMNE VDDLLQQVLE CDSAETLSYQ QAFIRHLDVD PLSADKIQLR EVAAKLDLSN
VADQEEDRDT LLQLLFTFGV EPNIGRDKPT FVYHFPASQA SLAQISTEDH RVAERFEVYY
KGIELANGFH ELTDAREQRM RFEQDNRKRA ALGLPQHPLD ENLLAALEHG LPDCSGVALG
VDRLIMLALK AERLSEVIAF PVDRA
//
