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SYFA_TREPS
ID   SYFA_TREPS              Reviewed;         553 AA.
AC   B2S4L0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00282};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00282};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00282};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00282};
GN   Name=pheS {ECO:0000255|HAMAP-Rule:MF_00282}; OrderedLocusNames=TPASS_0973;
OS   Treponema pallidum subsp. pallidum (strain SS14).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=455434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS14;
RX   PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA   Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA   Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA   Molla M.N., Albert T.J., Weinstock G.M.;
RT   "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT   determined with oligonucleotide arrays.";
RL   BMC Microbiol. 8:76-76(2008).
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_00282};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00282};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_00282};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00282}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00282}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00282}.
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DR   EMBL; CP000805; ACD71389.1; -; Genomic_DNA.
DR   RefSeq; WP_010882417.1; NC_021508.1.
DR   AlphaFoldDB; B2S4L0; -.
DR   SMR; B2S4L0; -.
DR   EnsemblBacteria; ACD71389; ACD71389; TPASS_0973.
DR   GeneID; 57879482; -.
DR   KEGG; tpp:TPASS_0973; -.
DR   PATRIC; fig|455434.6.peg.960; -.
DR   OMA; VHIKHPV; -.
DR   Proteomes; UP000001202; 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_00282; Phe_tRNA_synth_alpha2; 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; IPR022917; Phe_tRNA_ligase_alpha_bac/arc.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; SSF55681; 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; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..553
FT                   /note="Phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000114937"
FT   BINDING         400
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         479
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         481
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with beta subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
SQ   SEQUENCE   553 AA;  61233 MW;  E0D33A0FCDFDE3E1 CRC64;
     MMPRMTGKAD LNTLVHKLHP LEIKVLKNCA MDEILSTSLL ISRLGFKEGH ANQAFSWLRA
     KRIIEEHQRE QMRSFELTPC GYAAASDGTA EERMLTFLSS PPSLTAIADA AEHLHPRPPL
     CNGLSLPELA HALTLAPKDV GSAFGILAQE GILRMDGEKR IHIVSPHVSD RMSLTRTLLQ
     RAAARVASPS EASDTPPGTL FESELSDDER RVMERIAKKR GASDSLFKVS VRERVTFTFT
     PTARAVQEAL HTAGLTGNEI GALTVECLKS GAWKTQHLRR YNVHIPPARI IPGRSNAYAD
     FLEHIKDRLV ALGFQEFDGP LVETDFWNAD ALFMPQFHPA RDIHDVYYLK HPTHAPTIPE
     PFLSRVAATH ERGADSGSLG WRYSFDRDFT RRLLLRSQGT ALSARHLPTA HIPGKYFGIA
     RCFRHDQVDA THLADFYQTE GIVLGTDVNV CTLLGMLKIL ATEIAGAQEV RYVGGYFPFT
     EPSIELHALH PALGWFELGG AGLLRPEVTD PLGVHVPVMA WGLGVDRMAL LALGISDVRE
     LFSPDIESVR LRV
 
 
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