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Database: UniProt
Entry: J3YRJ3_9ENTR
LinkDB: J3YRJ3_9ENTR
Original site: J3YRJ3_9ENTR 
ID   J3YRJ3_9ENTR            Unreviewed;       325 AA.
AC   J3YRJ3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   08-NOV-2023, entry version 52.
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=A359_02970 {ECO:0000313|EMBL:AFP84693.1};
OS   secondary endosymbiont of Ctenarytaina eucalypti.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts.
OX   NCBI_TaxID=1199245 {ECO:0000313|EMBL:AFP84693.1, ECO:0000313|Proteomes:UP000003936};
RN   [1] {ECO:0000313|EMBL:AFP84693.1, ECO:0000313|Proteomes:UP000003936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ceuc_S {ECO:0000313|EMBL:AFP84693.1};
RX   PubMed=22821013; DOI=10.1093/molbev/mss180;
RA   Sloan D.B., Moran N.A.;
RT   "Genome reduction and co-evolution between the primary and secondary
RT   bacterial symbionts of psyllids.";
RL   Mol. Biol. Evol. 29:3781-3792(2012).
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}.
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DR   EMBL; CP003546; AFP84693.1; -; Genomic_DNA.
DR   RefSeq; WP_014887991.1; NC_018419.1.
DR   AlphaFoldDB; J3YRJ3; -.
DR   STRING; 1199245.A359_02970; -.
DR   KEGG; sect:A359_02970; -.
DR   PATRIC; fig|1199245.3.peg.358; -.
DR   HOGENOM; CLU_008255_1_1_6; -.
DR   OrthoDB; 9802326at2; -.
DR   Proteomes; UP000003936; 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   Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:AFP84693.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00174};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00174};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00174}; Reference proteome {ECO:0000313|Proteomes:UP000003936}.
FT   DOMAIN          19..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;  37173 MW;  CB92A9C37C34D808 CRC64;
     MNHSAKWQPS ASMSTLLKRN KIIQKIREFF SDRGFLEVET PAMSRATVTD VHLVSFQTRF
     IEPGATDGLS LYLITSPEYH MKRLLAAGSG PIFQICRSFR NEESGRYHNP EFTMLEWYRP
     NYDMYQLMHE VDDLLKIILS CSSVETFSYQ EAFTRYVGLD PLSVDKWKLY EAAVKWDLGN
     AISKEEDRDT LLQLLFSMMV EPKIGRDKIA FVYHFPASQA AMAAISTQDH RVAERFEVYF
     NGIELANGFH ELTDAPEQRQ RFEKDNRKLV EKGLTEKPID ENLLAALYQG MPACAGVALG
     VDRLVMLALK AECLSDVIAF PLERS
//
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