ID A7Z7F3_BACA2 Unreviewed; 345 AA.
AC A7Z7F3;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 01-MAY-2013, entry version 46.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
GN Name=pheS; OrderedLocusNames=RBAM_025710;
OS Bacillus amyloliquefaciens (strain FZB42).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=326423;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant
RT growth-promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(2007).
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 subunits (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
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DR EMBL; CP000560; ABS74929.1; -; Genomic_DNA.
DR RefSeq; YP_001422160.1; NC_009725.1.
DR ProteinModelPortal; A7Z7F3; -.
DR SMR; A7Z7F3; 83-343.
DR STRING; 326423.RBAM_025710; -.
DR EnsemblBacteria; ABS74929; ABS74929; RBAM_025710.
DR GeneID; 5463035; -.
DR KEGG; bay:RBAM_025710; -.
DR PATRIC; 18750266; VBIBacAmy31356_2606.
DR eggNOG; COG0016; -.
DR HOGENOM; HOG000242675; -.
DR KO; K01889; -.
DR OMA; LTHTPMF; -.
DR ProtClustDB; PRK00488; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:HAMAP.
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_ligase_II_N.
DR InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR010978; tRNA-bd_arm.
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 METAL 257 257 Magnesium (By similarity).
SQ SEQUENCE 345 AA; 38939 MW; 33923C2F99772D15 CRC64;
MMEEKLKQLE LEAAEKVEAA GSLKEVNDIR VQYLGKKGPI TEVLRGMGKL SAEERPKMGA
LANEVRERIA AAITAKNEQL EQEEMNKKLS SQTIDVTLPG SQVNIGGRHP LTVVIEEIED
LFIGMGYTVE EGPEVETDYY NFEALNLPKE HPARDMQDSF YITEEMLMRT QTSPVQTRTM
EKHKGKGPVK IICPGKVYRR DNDDATHSHQ FMQIEGLVVD RKISMSDLKG TLELVAKKMF
GQDREIRLRP SFFPFTEPSV EVDVTCFKCG GQGCSVCKKT GWIEILGAGM VHPNVLKMAG
FNPEEYQGFA FGMGVERIAM LKYGIEDIRH FYTNDVRFIS QFKQA
//
