(data stored in ACNUC7421 zone)

SWISSPROT: EPMA_PSEHT

ID   EPMA_PSEHT              Reviewed;         324 AA.
AC   Q3IFP4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 80.
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=PSHAa0475;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85572.1; -; Genomic_DNA.
DR   RefSeq; WP_011327185.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFP4; -.
DR   SMR; Q3IFP4; -.
DR   STRING; 326442.PSHAa0475; -.
DR   EnsemblBacteria; CAI85572; CAI85572; PSHAa0475.
DR   KEGG; pha:PSHAa0475; -.
DR   PATRIC; fig|326442.8.peg.452; -.
DR   eggNOG; ENOG4105CAP; Bacteria.
DR   eggNOG; COG2269; LUCA.
DR   HOGENOM; HOG000236579; -.
DR   KO; K04568; -.
DR   OMA; EWYRPGF; -.
DR   OrthoDB; POG091H04Y1; -.
DR   Proteomes; UP000006843; Chromosome I.
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; Q3IFP4.
DR   SWISS-2DPAGE; Q3IFP4.
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    324       Elongation factor P--(R)-beta-lysine
FT                                ligase.
FT                                /FTId=PRO_1000023628.
FT   NP_BIND      99    101       ATP. {ECO:0000255|HAMAP-Rule:MF_00174}.
FT   NP_BIND     243    244       ATP. {ECO:0000255|HAMAP-Rule:MF_00174}.
FT   REGION       75     77       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00174}.
FT   BINDING     108    108       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00174}.
FT   BINDING     117    117       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00174}.
FT   BINDING     250    250       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00174}.
FT   BINDING     299    299       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00174}.
SQ   SEQUENCE   324 AA;  36295 MW;  629881F0BC860BAF CRC64;
     MSVNLWAPSA SIATLKQRAV ILRSIREFFY ARNVMEVETP SLSGASVTDI HLVSFNTRFV
     GPGHASGLEL YLQTSPEFAM KRLLAAGSGP IFQLCKAFRN EEAGSHHNPE FTMLEWYRPG
     FDEFALMAEI DELMQLILDV APSERLTYQH AFEQVLGLDP LTASLEQLQQ LACEQGFADI
     AKNETHRDTL LQLLFCMKVE PTIGQHKPCF VYHFPASQAA LAQICDHDSR VAGRFELYYK
     NMELANGFNE LTNATEQAKR FNDDNEYRKQ NGLKQVPMDK HLIAALEHGL APCAGVALGI
     DRLVMLATQK SNIKEVIAFD VTRA
//

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