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Database: UniProt
Entry: A6PXK5_STRAG
LinkDB: A6PXK5_STRAG
Original site: A6PXK5_STRAG 
ID   A6PXK5_STRAG            Unreviewed;       151 AA.
AC   A6PXK5;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   24-JAN-2024, entry version 64.
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:CAK30066.1};
OS   Streptococcus agalactiae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1311 {ECO:0000313|EMBL:CAK30066.1};
RN   [1] {ECO:0000313|EMBL:CAK30066.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:LMG 14694 {ECO:0000313|EMBL:CAK30066.1};
RA   Naser S.M.;
RT   "PheS, rpoA and atpA based multilocus sequence analysis for a robust
RT   identification of Streptococcus.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAL18401.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMG 14847 {ECO:0000313|EMBL:CAL18401.1};
RA   Naser S.M.;
RT   "A robust identification system based on pheS, rpoA and atpA multilocus
RT   sequence analysis for Streptococcus.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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; AM269546; CAK30066.1; -; Genomic_DNA.
DR   EMBL; AM286821; CAL18401.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6PXK5; -.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490}.
FT   DOMAIN          1..108
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:CAK30066.1"
FT   NON_TER         151
FT                   /evidence="ECO:0000313|EMBL:CAK30066.1"
SQ   SEQUENCE   151 AA;  16909 MW;  45B08F3B4A0A5805 CRC64;
     DTFYITEEIL LRTHTSPVQA RTMDQHDFSK GPLKMISPGR VFRRDTDDAT HSHQFHQIEG
     LVVGENISMG DLKGTLQLIS QKMFGAERKI RLRPSYFPFT EPSVEVDVSC FKCGGKGCNV
     CKQTGWIEIL GAGMVHPSVL EMSGIDSEKY S
//
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