ID   SYFB_HAEIN              Reviewed;         795 AA.
AC   P43820;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE            Short=PheRS;
GN   Name=pheT; OrderedLocusNames=HI_1312;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 1 subfamily. {ECO:0000305}.
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DR   EMBL; L42023; AAC22958.1; -; Genomic_DNA.
DR   PIR; I64115; I64115.
DR   RefSeq; NP_439463.1; NC_000907.1.
DR   RefSeq; WP_005694456.1; NC_000907.1.
DR   AlphaFoldDB; P43820; -.
DR   SMR; P43820; -.
DR   STRING; 71421.HI_1312; -.
DR   BindingDB; P43820; -.
DR   EnsemblBacteria; AAC22958; AAC22958; HI_1312.
DR   KEGG; hin:HI_1312; -.
DR   PATRIC; fig|71421.8.peg.1364; -.
DR   eggNOG; COG0072; Bacteria.
DR   eggNOG; COG0073; Bacteria.
DR   HOGENOM; CLU_016891_0_0_6; -.
DR   OMA; ISYNWLK; -.
DR   PhylomeDB; P43820; -.
DR   BioCyc; HINF71421:G1GJ1-1337-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   CDD; cd00769; PheRS_beta_core; 1.
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; 1.
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   TIGRFAMs; TIGR00472; pheT_bact; 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;
KW   Reference proteome; RNA-binding; tRNA-binding.
FT   CHAIN           1..795
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_0000126892"
FT   DOMAIN          39..148
FT                   /note="tRNA-binding"
FT   DOMAIN          401..476
FT                   /note="B5"
FT   DOMAIN          701..794
FT                   /note="FDX-ACB"
FT   BINDING         454
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
FT   BINDING         463
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   795 AA;  86747 MW;  470FE3F404F6673D CRC64;
     MKFSEQWVRE WVNPAVSTEQ LCEQITMLGL EVDGVEAVAG TFNGVVVGEV VECAQHPDAD
     KLRVTKVNVG GDRLLDIVCG APNCRQGLKV ACATEGAVLP GDFKIKKTKL RGQPSEGMLC
     SFSELGIDVE ADGIIELPLD APIGTDLREY LALDDNAIEI SLTPNRADCL SIAGIAREIG
     VVNKQLVNQL HFEAAPATIS DKVQIDLQAP EACPRYLLRV IKNVNVKAPS PMWMQEKLRR
     CGIRSIDPIV DITNYILLEF GQPMHAFDAA KVTQPVQVRF AKEGEELVLL DGSTAKLQSN
     TLLIADQNGP LAMAGIFGGA ASGVNSETKD VILESAFFAP LAIAGRARQY GLHTDASHRF
     ERGVDFELAR KAMERATALL LEICGGEAGE ICEASSETHL PKVNTVQLRR SKLDALLGHH
     IETGSVTEIF HRLGFDVTYA NDIWTVTSAS WRFDIEIEED LIEEVARIYG YNSIPNNAPL
     AHLCMREHKE SDLDLARIKT ALVDADYQEA ITYSFVDPKI QSLLHPHQEA LVLPNPISVE
     MSAMRVSLIS GLLGAVLYNQ NRQQSRVRLF ETGLRFVPDA NAEFGVRQEF VLSAVITGTA
     KSEHWAGKAE SVDFFDLKGD LESVLSLTEG GHRVRFVAKQ FDALHPGQSA AIELDGQEIG
     FIGAIHPSIS QKLGLNGKTF VFEILWNAIA ARNVVQAKEI SKFPANRRDL ALVVADSVPA
     GELIAACKQA GGEKLVQVNL FDVYQGVGVA EGYKSLAISL TVQDNEKTLE DEEINAVISA
     VLAEVKQRFN AELRD