ID   SYFB_TROW8              Reviewed;         961 AA.
AC   Q83HH4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00283};
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00283};
GN   Name=pheT {ECO:0000255|HAMAP-Rule:MF_00283}; OrderedLocusNames=TW604;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
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_00283};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00283};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_00283};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00283}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00283}.
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DR   EMBL; BX251412; CAD67269.1; -; Genomic_DNA.
DR   RefSeq; WP_011096549.1; NC_004551.1.
DR   AlphaFoldDB; Q83HH4; -.
DR   SMR; Q83HH4; -.
DR   GeneID; 67388386; -.
DR   KEGG; tws:TW604; -.
DR   HOGENOM; CLU_016891_0_0_11; -.
DR   OMA; ISYNWLK; -.
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:UniProtKB-KW.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd02796; tRNA_bind_bactPheRS; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.70.380; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.50.40.10; -; 1.
DR   HAMAP; MF_00283; Phe_tRNA_synth_beta1; 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; IPR005121; Fdx_antiC-bd.
DR   InterPro; IPR036690; Fdx_antiC-bd_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bact.
DR   InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR   InterPro; IPR041616; PheRS_beta_core.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR033714; tRNA_bind_bactPheRS.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   PANTHER; PTHR10947; PTHR10947; 2.
DR   Pfam; PF03483; B3_4; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF03147; FDX-ACB; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   Pfam; PF17759; tRNA_synthFbeta; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SMART; SM00896; FDX-ACB; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54991; SSF54991; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   PROSITE; PS51483; B5; 1.
DR   PROSITE; PS51447; FDX_ACB; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis; RNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..961
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_0000232829"
FT   DOMAIN          85..201
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          456..538
FT                   /note="B5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          869..960
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   REGION          621..674
FT                   /note="Insert"
FT   BINDING         516
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         522
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         525
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         526
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
SQ   SEQUENCE   961 AA;  104858 MW;  FBA3889DE5CE13DA CRC64;
     MAVLRVPVSW LLEYVHTQTG FVGETGIRSD TRRTHTDCPV AEDILESLLS VGFEGEILDR
     PELSGPIVVG RVLDFTEEVH SNGKTIRWCK VRVCAPVQPN NTPLSKDCNP STQTGNFSNA
     DTNSALETRD IVCGASNFSK GDLVVVTLPG SNLPGGFHVT ARKVYGHLSD GMIASEKELG
     VGDNHDGILR LAEVFQGDEL SKIREGDNAL ELLALTDSAV AVSITPDRGY AMSIRGIARE
     YALANNIPFS DPLPDDVLPA GGLSIDLRCK PNAFFTLLIQ EIENNQTPQW MVRRLQLAGI
     RSVCPVVDIT NYVMVETGQP LHAYDYDAIQ GSLCVRTADK KETLDTIDGR RLELHTDDLV
     VADANGALSL AGVIGGSRSR VTSDTKRILL EAGNFNPIDI SLSSRRHKLY TEASARFARS
     VDILIAQRAL ARAAELIRDL ASGDITELGS AYINYTQQSP ILLSTLDIER VVGCCFTREE
     IMSSLRAIGC DVSCDSDHST PDTQVMLVTP PSFRPDLVNV QDLAEEVIRV IGFNRIPSLR
     LSVPHREQPV QSQQYKLENG KLENGYTLSP VTPPRTPPVT FEQRRLLGQS LAACGHVEVI
     CYPFVNLAAA GICHIDVTHN PDSTHNPDSG SDPIIPTGVT RITEPGSSGV SGPDNVDVKE
     KCSADTSVEH PTTRAISLHN PIDATEGYLR RSLIPGLLQC AHRNLSRGLC DLSIFEIGRV
     FLGQLRTSNL IGCNSDSTCN ACSRKNTIES MNEVYQPYTV SVLQTGSAIQ KQPYTEGRKY
     DLADVFDSAR QIARGLGVDF HFVQDKHPAF HPGRCAKVIC KHHHIGYTGQ ILPTLANKHN
     LPDNVFACEI NLDLVAQLGC SQEIVKTLPT SPAATQHLTL TLGNNIAAAS VISVVKEGAG
     ELLEDIRLID EYKHEESDKK SLTFAMRFRD KEKTLTAQRV NLAKENAVRL ASSKFGAIMR
     R