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Database: UniProt
Entry: A9JQ12_9LACO
LinkDB: A9JQ12_9LACO
Original site: A9JQ12_9LACO 
ID   A9JQ12_9LACO            Unreviewed;       132 AA.
AC   A9JQ12;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE   Flags: Fragment;
GN   Name=pheS {ECO:0000313|EMBL:CAP16832.1};
OS   Pediococcus parvulus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=54062 {ECO:0000313|EMBL:CAP16832.1};
RN   [1] {ECO:0000313|EMBL:CAP16832.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LAB 299 {ECO:0000313|EMBL:CAP16839.1}, and Type strain: LMG
RC   11486 {ECO:0000313|EMBL:CAP16832.1};
RA   De Bruyne K., Franz C.M., Vancanneyt M., Schillinger U., Mozzi F.,
RA   de Valdez G.F., De Vuyst L., Vandamme P.;
RT   "Pediococcus argentinicus sp. nov. from Argentinean fermented wheat flour
RT   and identification of Pediococcus species by pheS, rpoA and atpA sequence
RT   analysis.";
RL   Int. J. Syst. Evol. Microbiol. 58:2909-2916(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:0000256|ARBA:ARBA00000395};
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DR   EMBL; AM899829; CAP16832.1; -; Genomic_DNA.
DR   EMBL; AM899836; CAP16839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9JQ12; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:CAP16832.1};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000313|EMBL:CAP16832.1}.
FT   DOMAIN          1..118
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAP16832.1"
FT   NON_TER         132
FT                   /evidence="ECO:0000313|EMBL:CAP16832.1"
SQ   SEQUENCE   132 AA;  14976 MW;  E2E85D452A7E71F6 CRC64;
     QDTFYITDEI LMRSQTSPVQ ARTMEKHDFS KGPLKMISPG VVYRRDTDDA THSHQFHQVE
     GLVIDKHITM GDLKGTLETL AKELFGDRFE VRLRPSYFPF TEPSVEADVT CFNCMGKGCS
     VCKQTGWIEV LG
//
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