ID   SYK3_ECOUT              Reviewed;         325 AA.
AC   Q1R3A2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Putative lysyl-tRNA synthetase;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysine--tRNA ligase;
DE            Short=LysRS;
DE   AltName: Full=GX;
GN   Name=poxA; OrderedLocusNames=UTI89_C4755;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Could be a lysyl-tRNA synthetase.
CC   -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate
CC       + L-lysyl-tRNA(Lys).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000243; ABE10162.1; -; Genomic_DNA.
DR   RefSeq; YP_543693.1; -.
DR   GeneID; 3991003; -.
DR   GenomeReviews; CP000243_GR; UTI89_C4755.
DR   KEGG; eci:UTI89_C4755; -.
DR   HOGENOM; Q1R3A2; -.
DR   OMA; Q1R3A2; VFRNEEA.
DR   BioCyc; ECOL364106:UTI89_C4755-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00174; -; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004525; Lys-tRNA-synth-rel.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 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;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    325       Putative lysyl-tRNA synthetase.
FT                                /FTId=PRO_1000023621.
SQ   SEQUENCE   325 AA;  36976 MW;  F72B535CCA23E4CC CRC64;
     MSETASWQPS ASIPNLLKRA AIMAEIRRFF ADRGVLEVET PCMSQATVTD IHLVPFETRF
     VGPGHSQGMN LWLMTSPEYH MKRLLVAGCG PVFQLCRSFR NEEMGRYHNP EFTMLEWYRP
     HYDMYRLMNE VDDLLQQVLD CPAAESLSYQ QAFLRYLEID PLSADKTQLR EVAAKLDLSN
     VADTEEDRDT LLQLLFTFGV EPNIGKEKPT FVYHFPASQA SLAQISTEDH RVAERFEVYY
     KGIELANGFH ELTDAREQQQ RFEQDNRKRA ARGLPQHPID QNLIEALKVG MPDCSGVALG
     VDRLVMLALG AETLAEVIAF SVDRA
//