(data stored in ACNUC7421 zone)

SWISSPROT: EPMA_EDWI9

ID   EPMA_EDWI9              Reviewed;         325 AA.
AC   C5BDL9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 44.
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=NT01EI_0394;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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
CC       (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine
CC       produced by EpmB, forming a lysyl-adenylate, from which the beta-
CC       lysyl moiety is then transferred to the epsilon-amino group of a
CC       conserved specific lysine residue in EF-P. {ECO:0000255|HAMAP-
CC       Rule:MF_00174}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00174}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. EpmA subfamily. {ECO:0000255|HAMAP-Rule:MF_00174}.
DR   EMBL; CP001600; ACR67635.1; -; Genomic_DNA.
DR   RefSeq; WP_015869841.1; NC_012779.2.
DR   SMR; C5BDL9; -.
DR   STRING; 634503.NT01EI_0394; -.
DR   EnsemblBacteria; ACR67635; ACR67635; NT01EI_0394.
DR   GeneID; 7961222; -.
DR   KEGG; eic:NT01EI_0394; -.
DR   PATRIC; fig|634503.3.peg.357; -.
DR   eggNOG; ENOG4105CAP; Bacteria.
DR   eggNOG; COG2269; LUCA.
DR   HOGENOM; HOG000236579; -.
DR   KO; K04568; -.
DR   OMA; EWYRPGF; -.
DR   OrthoDB; POG091H04Y1; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR004525; EpmA.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   PANTHER; PTHR42918:SF7; PTHR42918:SF7; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   TIGRFAMs; TIGR00462; genX; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BDL9.
DR   SWISS-2DPAGE; C5BDL9.
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    325       Elongation factor P--(R)-beta-lysine
FT                                ligase.
FT                                /FTId=PRO_1000203723.
FT   NP_BIND     100    102       ATP. {ECO:0000255|HAMAP-Rule:MF_00174}.
FT   NP_BIND     244    245       ATP. {ECO:0000255|HAMAP-Rule:MF_00174}.
FT   REGION       76     78       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00174}.
FT   BINDING     109    109       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00174}.
FT   BINDING     118    118       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00174}.
FT   BINDING     251    251       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00174}.
FT   BINDING     300    300       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00174}.
SQ   SEQUENCE   325 AA;  36803 MW;  BB122D20F9D556E6 CRC64;
     MSDMASWQPS APVANLLKRA SILSTIRRFF SDRGVLEVDT PSMSQATVTD VHLVPFQTHF
     VGPGVAQGMM LYLMTSPEYH MKRLLAAGSG PIYQLCRSFR NEESGRYHNP EFTMLEWYRP
     HYDMYRLMNE VDDLLQQVLE CESAETLSYQ QAFIRHLDVD PLSADKTQLR EVAAKLDLSN
     VADNEEDRDT LLQLLFAFGV EPHIGKERPV FVYHFPASQA SLAQISTEDH RVAERFEVYY
     RGVELANGFH ELTDAAEQRQ RFEQDNRKRA AAGLPQQPID EHLLAALEHG MPDSSGVALG
     VDRLIMLALS AERLSEVIAF SVDRA
//

If you have problems or comments...

PBIL Back to PBIL home page