ID   SYFA_STAAW              Reviewed;         352 AA.
AC   P68850; Q99QR1;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-JAN-2012, entry version 49.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha chain;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha chain;
DE            Short=PheRS;
GN   Name=pheS; OrderedLocusNames=MW1021;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   MEDLINE=22040717; PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA   Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA   Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-
RT   acquired MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC       diphosphate + L-phenylalanyl-tRNA(Phe).
CC   -!- COFACTOR: Binds 2 magnesium ions per tetramer (By similarity).
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Phe-tRNA synthetase alpha chain type 1 subfamily.
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DR   EMBL; BA000033; BAB94886.1; -; Genomic_DNA.
DR   RefSeq; NP_645838.1; NC_003923.1.
DR   ProteinModelPortal; P68850; -.
DR   SMR; P68850; 84-351.
DR   STRING; P68850; -.
DR   EnsemblBacteria; EBSTAT00000027038; EBSTAP00000026077; EBSTAG00000027037.
DR   GeneID; 1003133; -.
DR   GenomeReviews; BA000033_GR; MW1021.
DR   KEGG; sam:MW1021; -.
DR   PATRIC; 19568622; VBIStaAur44266_1070.
DR   eggNOG; COG0016; -.
DR   GeneTree; EBGT00050000024011; -.
DR   HOGENOM; HBG284353; -.
DR   OMA; FRASYFP; -.
DR   PhylomeDB; P68850; -.
DR   ProtClustDB; PRK00488; -.
DR   BioCyc; SAUR196620:MW1021-MONOMER; -.
DR   BindingDB; P68850; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR   HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1; -.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR004188; Phe-tRNA_synth_II_N.
DR   InterPro; IPR022911; Phe_tRNA_synth_alpha1_bac.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   KO; K01889; -.
DR   Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF46589; tRNA_binding_arm; 1.
DR   TIGRFAMs; TIGR00468; PheS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    352       Phenylalanine--tRNA ligase alpha chain.
FT                                /FTId=PRO_0000126765.
FT   METAL       258    258       Magnesium (By similarity).
SQ   SEQUENCE   352 AA;  40121 MW;  01FD437729B8FDF7 CRC64;
     MSEQQTMSEL KQQALVDINE ANDERALQEV KVKYLGKKGS VSGLMKLMKD LPNEEKPAFG
     QKVNELRQTI QNELDERQQM LVKEKLNKQL AEETIDVSLP GRHIEIGSKH PLTRTIEEIE
     DLFLGLGYEI VNGYEVEQDH YNFEMLNLPK SHPARDMQDS FYITDEILLR THTSPVQART
     MESRHGQGPV KIICPGKVYR RDSDDATHSH QFTQIEGLVV DKNVKMSDLK GTLELLAKKL
     FGADREIRLR PSYFPFTEPS VEVDVSCFKC KGKGCNVCKH TGWIEILGAG MVHPNVLEMA
     GFDSSEYSGF AFGMGPDRIA MLKYGIEDIR HFYTNDVRFL DQFKAVEDRG DM
//