ID SYFA_LACDA Reviewed; 349 AA.
AC Q1G9C7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 01-MAY-2013, entry version 55.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE Short=PheRS;
GN Name=pheS; OrderedLocusNames=Ldb1487;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM
OS 20081).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K.,
RA Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V.,
RA Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T.,
RA Gibrat J.-F., Bessieres P., Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals
RT extensive and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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; CR954253; CAI98287.1; -; Genomic_DNA.
DR RefSeq; YP_619313.1; NC_008054.1.
DR ProteinModelPortal; Q1G9C7; -.
DR SMR; Q1G9C7; 81-349.
DR STRING; 390333.Ldb1487; -.
DR EnsemblBacteria; CAI98287; CAI98287; Ldb1487.
DR GeneID; 4085057; -.
DR KEGG; ldb:Ldb1487; -.
DR PATRIC; 22218442; VBILacDel123523_1338.
DR eggNOG; COG0016; -.
DR HOGENOM; HOG000242675; -.
DR KO; K01889; -.
DR OMA; LTHTPMF; -.
DR ProtClustDB; PRK00488; -.
DR BioCyc; LDEL390333:GIXG-1467-MONOMER; -.
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 CHAIN 1 349 Phenylalanine--tRNA ligase alpha subunit.
FT /FTId=PRO_1000006848.
FT METAL 259 259 Magnesium (By similarity).
SQ SEQUENCE 349 AA; 39747 MW; 947B935DD993F30B CRC64;
MDLFDRLKEL REQGLAEIKE AESEKSLNDV RVKLVGKKGE LTQILHQMKD VAPEKRREVG
QKVNELRDLF NENLASAKDN LIEKAIEARL EAEKIDVTLP GRRKHVGSKH PIRIIQDDLE
RFFIGMGYQV VQGPEIESEH YNFEMLNLPK DHPARDMQAT FYVDADHLLR SQTSPVQART
MEKHDFDKGD LKMISPGKVY RRDDDDATHS HQFMQMEGLV VGKNISLSDL KGTLELVAKH
EFGQDRETRL RPSYFPFTEP SVEMDVSCFE CGGKGCAICK NTGWIEVLGA GIVHPNVLSA
AGIDPSVYSG FAFGLGLDRF AILKYGIDDI RDFYSDDVRF LQQFRQEED
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