ID   SYK3_ECOLI              Reviewed;         325 AA.
AC   P0A8N7; P03812; P78141; Q2M6E7; Q8XDP9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   16-JUN-2009, entry version 39.
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; Synonyms=genX, yjeA; OrderedLocusNames=b4155, JW4116;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92104501; PubMed=1761227; DOI=10.1016/0378-1119(91)90503-4;
RA   Kong L., Fromant M., Blanquet S., Plateau P.;
RT   "Evidence for a new Escherichia coli protein resembling a lysyl-tRNA
RT   synthetase.";
RL   Gene 108:163-164(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=95334362; PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
RA   Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the
RT   region from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152.
RX   MEDLINE=82138876; PubMed=7037404;
RA   Cole S.T.;
RT   "Nucleotide sequence coding for the flavoprotein subunit of the
RT   fumarate reductase of Escherichia coli.";
RL   Eur. J. Biochem. 122:479-484(1982).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=6286595;
RA   Chang Y.-Y., Cronan J.E. Jr.;
RT   "Mapping nonselectable genes of Escherichia coli by using transposon
RT   Tn10: location of a gene affecting pyruvate oxidase.";
RL   J. Bacteriol. 151:1279-1289(1982).
RN   [7]
RP   SIMILARITY TO CLASS-II AA-TRNA SYNTHETASES.
RX   MEDLINE=89345597; PubMed=2668951; DOI=10.1073/pnas.86.16.6023;
RA   Gampel A., Tzagoloff A.;
RT   "Homology of aspartyl- and lysyl-tRNA synthetases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:6023-6027(1989).
CC   -!- FUNCTION: Could be a lysyl-tRNA synthetase.
CC   -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate
CC       + L-lysyl-tRNA(Lys).
CC   -!- INTERACTION:
CC       P0AFG8:aceE; NbExp=1; IntAct=EBI-562598, EBI-542683;
CC   -!- DISRUPTION PHENOTYPE: Cell have a reduced pyruvate oxidase
CC       activity and a reduced growth rate.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; X59988; CAA42604.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97054.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC77115.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78159.1; -; Genomic_DNA.
DR   EMBL; J01611; AAA23436.2; -; Genomic_DNA.
DR   PIR; S56383; S56383.
DR   RefSeq; AP_004658.1; -.
DR   RefSeq; NP_418579.2; -.
DR   HSSP; P14825; 1E1O.
DR   IntAct; P0A8N7; 3.
DR   GeneID; 948672; -.
DR   GenomeReviews; AP009048_GR; JW4116.
DR   GenomeReviews; U00096_GR; b4155.
DR   KEGG; ecj:JW4116; -.
DR   KEGG; eco:b4155; -.
DR   EchoBASE; EB1196; -.
DR   EcoGene; EG11211; poxA.
DR   HOGENOM; P0A8N7; -.
DR   OMA; P0A8N7; VFRNEEA.
DR   BioCyc; EcoCyc:EG11211-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:0005515; F:protein binding; IPI:IntAct.
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   1: Evidence at protein level;
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_0000152719.
FT   CONFLICT     78     78       E -> Q (in Ref. 5; AAA23436).
FT   CONFLICT    144    144       A -> E (in Ref. 5; AAA23436).
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
//