ID   SYFB_BORBZ              Reviewed;         566 AA.
AC   B7J278;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00284};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00284};
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00284};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00284};
GN   Name=pheT {ECO:0000255|HAMAP-Rule:MF_00284}; OrderedLocusNames=BbuZS7_0524;
OS   Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=445985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS7;
RX   PubMed=20935092; DOI=10.1128/jb.01158-10;
RA   Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA   Mongodin E.F., Luft B.J.;
RT   "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL   J. Bacteriol. 193:1018-1020(2011).
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_00284};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00284};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00284}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00284}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00284}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001205; ACK75091.1; -; Genomic_DNA.
DR   RefSeq; WP_012597403.1; NC_011728.1.
DR   AlphaFoldDB; B7J278; -.
DR   SMR; B7J278; -.
DR   EnsemblBacteria; ACK75091; ACK75091; BbuZS7_0524.
DR   KEGG; bbz:BbuZS7_0524; -.
DR   HOGENOM; CLU_020279_3_0_12; -.
DR   OMA; FPGRCAN; -.
DR   OrthoDB; 53568at2; -.
DR   Proteomes; UP000006901; 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:InterPro.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.50.40.10; -; 1.
DR   HAMAP; MF_00284; Phe_tRNA_synth_beta2; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc_euk.
DR   InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR   InterPro; IPR022918; Phe_tRNA_ligase_beta2_arc.
DR   InterPro; IPR041616; PheRS_beta_core.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   PANTHER; PTHR10947; PTHR10947; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF17759; tRNA_synthFbeta; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00471; pheT_arch; 1.
DR   PROSITE; PS51483; B5; 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..566
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_1000119403"
FT   DOMAIN          287..362
FT                   /note="B5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT   BINDING         340
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT   BINDING         346
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT   BINDING         349
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT   BINDING         350
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
SQ   SEQUENCE   566 AA;  65168 MW;  AD03BA0D86118E7D CRC64;
     MPKLEIYKNL FLDKIGKNFT NLEISELLEP FKAEFDGFDE SSGKIKIEFN DTNRPDLWSY
     LGLARQIKTY FFGEMPYYDF FSKKGDFKKF YGEILVDGKM SQIRPFIFGF LAKGLIINDK
     MLETLIQFQE KLCQNYGQKR RRIAMGMYNS NFIKFPISYI ASSPNHKFVP LGMDYELSLL
     EINEKHPKGL EYSHIIKNFD KFPLLLDDNN NVVSYPPIIN SNNIGSLKVG DTDLFVEVTG
     IDFEATLLAL SIAACDFYDM GFEILPVKTV FREPFNLDFK ELVCPYYFQE EVEFNVENIN
     RLLGSNLTLE RICLSLKKMG VNSYSKDFKN YIVPPFYRND FLHEVDVIED VMIGEGLSSF
     NPELPKAFAV GRLSPLEEFS RNVRNLMVGM GFQEMIYNYM GSKKDFIDRM NINDQNFLKV
     SNPMTENYEY IRASIIPNLL KSESVSSNFP YPHKIFEIGK VALRNLDTTE GTSTFTNLAF
     LMSGKEISFN EINSIVATLF YYLNIEINLI ESKTTFYING RGADIVIEGF NIGGFGEISP
     YVLNNFGIFI PCSVFEVNIN KLMSRS