SYFA_STAHJ
ID SYFA_STAHJ Reviewed; 352 AA.
AC Q4L5E3;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00281};
DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00281};
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00281};
DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00281};
GN Name=pheS {ECO:0000255|HAMAP-Rule:MF_00281}; OrderedLocusNames=SH1823;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00281};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00281};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC Rule:MF_00281};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00281}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00281}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 1 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00281}.
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DR EMBL; AP006716; BAE05132.1; -; Genomic_DNA.
DR RefSeq; WP_011276100.1; NC_007168.1.
DR PDB; 2RHQ; X-ray; 2.20 A; A=84-351.
DR PDB; 2RHS; X-ray; 2.20 A; A/C=84-351.
DR PDBsum; 2RHQ; -.
DR PDBsum; 2RHS; -.
DR AlphaFoldDB; Q4L5E3; -.
DR SMR; Q4L5E3; -.
DR STRING; 279808.SH1823; -.
DR DrugBank; DB07817; 1-{3-[(4-pyridin-2-ylpiperazin-1-yl)sulfonyl]phenyl}-3-(1,3-thiazol-2-yl)urea.
DR PRIDE; Q4L5E3; -.
DR EnsemblBacteria; BAE05132; BAE05132; SH1823.
DR GeneID; 58062054; -.
DR KEGG; sha:SH1823; -.
DR eggNOG; COG0016; Bacteria.
DR HOGENOM; CLU_025086_0_1_9; -.
DR OMA; DWHNFTA; -.
DR OrthoDB; 469058at2; -.
DR EvolutionaryTrace; Q4L5E3; -.
DR Proteomes; UP000000543; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR004530; Phe-tRNA-synth_IIc_mito.
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 PANTHER; PTHR11538:SF41; PTHR11538:SF41; 1.
DR Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00468; pheS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..352
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000232028"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with beta subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00281"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 190..199
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 210..223
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 226..241
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 257..266
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:2RHS"
FT TURN 276..280
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 281..292
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:2RHS"
SQ SEQUENCE 352 AA; 40138 MW; B3C516F1D4A223E7 CRC64;
MTQNDSMAEL KQQALVDINE AQNERELQDV KVKYLGKKGS VSGLMKNMKD LPNEEKPAYG
QKVNELRQTI QKELDEKQEL LKNEKLNQQL AEETIDVTLP SRQISIGSKH PLTRTVEEIE
DLFLGLGYEI VDGYEVEQDY YNFEALNLPK SHPARDMQDS FYITDEILMR THTSPVQART
MEKRNGQGPV KIICPGKVYR RDSDDATHSH QFTQIEGLVV DKNIKMSDLK GTLELVAKKL
FGADREIRLR PSYFPFTEPS VEVDVSCFKC KGKGCNVCKH TGWIEILGAG MVHPNVLEMA
GFDSNEYSGF AFGMGPDRIA MLKYGIEDIR YFYTNDVRFL EQFKAVEDRG EA
