SYFA_ECOLI
ID SYFA_ECOLI Reviewed; 327 AA.
AC P08312; P78233; Q59406;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 197.
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=b1714, JW5277;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6317865; DOI=10.1016/0022-2836(83)90092-x;
RA Fayat G., Mayaux J.-F., Sacerdot C., Fromant M., Springer M.,
RA Grunberg-Manago M., Blanquet S.;
RT "Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for
RT an attenuation mechanism. Identification of the gene for the ribosomal
RT protein L20.";
RL J. Mol. Biol. 171:239-261(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Miller H.I.;
RL Submitted (NOV-1986) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 254-327.
RX PubMed=2991205; DOI=10.1128/jb.163.2.787-791.1985;
RA Mechulman Y., Fayat G., Blanquet S.;
RT "Sequence of the Escherichia coli pheST operon and identification of the
RT himA gene.";
RL J. Bacteriol. 163:787-791(1985).
RN [7]
RP SEQUENCE REVISION TO 74, AND MUTAGENESIS OF ALA-294.
RX PubMed=1942071; DOI=10.1016/0022-2836(91)90740-w;
RA Kast P., Hennecke H.;
RT "Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA
RT synthetase altered by distinct mutations.";
RL J. Mol. Biol. 222:99-124(1991).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP VARIANT ASP-191.
RX PubMed=1959653; DOI=10.1016/0014-5793(91)81176-9;
RA Kast P., Wehrli C., Hennecke H.;
RT "Impaired affinity for phenylalanine in Escherichia coli phenylalanyl-tRNA
RT synthetase mutant caused by Gly-to-Asp exchange in motif 2 of class II tRNA
RT synthetases.";
RL FEBS Lett. 293:160-163(1991).
RN [10]
RP VARIANT PHES5 ASP-98.
RX PubMed=1537809; DOI=10.1128/jb.174.5.1686-1689.1992;
RA Kast P., Keller B., Hennecke H.;
RT "Identification of the pheS5 mutation, which causes thermosensitivity of
RT Escherichia coli mutant NP37.";
RL J. Bacteriol. 174:1686-1689(1992).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000250};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC -!- INTERACTION:
CC P08312; P0AD99: brnQ; NbExp=5; IntAct=EBI-555676, EBI-555687;
CC P08312; P39176: erfK; NbExp=4; IntAct=EBI-555676, EBI-555707;
CC P08312; P07395: pheT; NbExp=9; IntAct=EBI-555676, EBI-555713;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23564.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; V00291; CAA23564.1; ALT_INIT; Genomic_DNA.
DR EMBL; K02844; AAA51469.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74784.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15482.2; -; Genomic_DNA.
DR PIR; B64930; SYECFA.
DR RefSeq; NP_416229.1; NC_000913.3.
DR RefSeq; WP_000018596.1; NZ_STEB01000009.1.
DR PDB; 3PCO; X-ray; 3.02 A; A/C=1-327.
DR PDB; 6OZ5; X-ray; 2.50 A; A/C=2-327.
DR PDB; 6P24; X-ray; 2.12 A; A/C=2-327.
DR PDB; 6P26; X-ray; 3.16 A; A/C=2-327.
DR PDBsum; 3PCO; -.
DR PDBsum; 6OZ5; -.
DR PDBsum; 6P24; -.
DR PDBsum; 6P26; -.
DR AlphaFoldDB; P08312; -.
DR SMR; P08312; -.
DR BioGRID; 4260287; 264.
DR BioGRID; 850583; 8.
DR ComplexPortal; CPX-5222; Phenylalanyl-tRNA synthetase complex.
DR DIP; DIP-6878N; -.
DR IntAct; P08312; 7.
DR STRING; 511145.b1714; -.
DR DrugCentral; P08312; -.
DR SWISS-2DPAGE; P08312; -.
DR jPOST; P08312; -.
DR PaxDb; P08312; -.
DR PRIDE; P08312; -.
DR EnsemblBacteria; AAC74784; AAC74784; b1714.
DR EnsemblBacteria; BAA15482; BAA15482; BAA15482.
DR GeneID; 66674392; -.
DR GeneID; 946223; -.
DR KEGG; ecj:JW5277; -.
DR KEGG; eco:b1714; -.
DR PATRIC; fig|1411691.4.peg.543; -.
DR EchoBASE; EB0703; -.
DR eggNOG; COG0016; Bacteria.
DR HOGENOM; CLU_025086_0_1_6; -.
DR InParanoid; P08312; -.
DR OMA; DWHNFTA; -.
DR PhylomeDB; P08312; -.
DR BioCyc; EcoCyc:PHES-MON; -.
DR BioCyc; MetaCyc:PHES-MON; -.
DR BRENDA; 6.1.1.20; 2026.
DR SABIO-RK; P08312; -.
DR PRO; PR:P08312; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IDA:EcoCyc.
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; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IDA:ComplexPortal.
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;
KW Reference proteome.
FT CHAIN 1..327
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000126701"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with beta subunit"
FT /evidence="ECO:0000250"
FT VARIANT 98
FT /note="G -> D (in thermosensitive mutant pheS5; might cause
FT subunit disaggregation due to electrostatic repulsion)"
FT /evidence="ECO:0000269|PubMed:1537809"
FT VARIANT 191
FT /note="G -> D (decreased affinity for Phe)"
FT /evidence="ECO:0000269|PubMed:1959653"
FT CONFLICT 74
FT /note="R -> A (in Ref. 2; CAA23564 and 4; AAA51469)"
FT /evidence="ECO:0000305"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:6P24"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:6P24"
FT HELIX 27..42
FT /evidence="ECO:0007829|PDB:6P24"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:6P24"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6P24"
FT HELIX 53..86
FT /evidence="ECO:0007829|PDB:6P24"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:3PCO"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:6P24"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:6P24"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:6P24"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:6P24"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:6P24"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3PCO"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:6P24"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:6P24"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6OZ5"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:6P24"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:6P24"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6OZ5"
FT STRAND 204..217
FT /evidence="ECO:0007829|PDB:6P24"
FT HELIX 220..235
FT /evidence="ECO:0007829|PDB:6P24"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:6P24"
FT STRAND 251..260
FT /evidence="ECO:0007829|PDB:6P24"
FT STRAND 264..275
FT /evidence="ECO:0007829|PDB:6P24"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:6P24"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:6P24"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:6P24"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:6P24"
FT HELIX 313..317
FT /evidence="ECO:0007829|PDB:6P24"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:6P24"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:6P24"
SQ SEQUENCE 327 AA; 36832 MW; 601082304FD27110 CRC64;
MSHLAELVAS AKAAISQASD VAALDNVRVE YLGKKGHLTL QMTTLRELPP EERPAAGAVI
NEAKEQVQQA LNARKAELES AALNARLAAE TIDVSLPGRR IENGGLHPVT RTIDRIESFF
GELGFTVATG PEIEDDYHNF DALNIPGHHP ARADHDTFWF DTTRLLRTQT SGVQIRTMKA
QQPPIRIIAP GRVYRNDYDQ THTPMFHQME GLIVDTNISF TNLKGTLHDF LRNFFEEDLQ
IRFRPSYFPF TEPSAEVDVM GKNGKWLEVL GCGMVHPNVL RNVGIDPEVY SGFAFGMGME
RLTMLRYGVT DLRSFFENDL RFLKQFK
