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SYFB_CORDI
ID   SYFB_CORDI              Reviewed;         836 AA.
AC   Q6NHH1;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=DIP1166;
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=257309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA   Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA   De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA   Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA   Parkhill J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(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; BX248357; CAE49686.1; -; Genomic_DNA.
DR   RefSeq; WP_010934854.1; NC_002935.2.
DR   AlphaFoldDB; Q6NHH1; -.
DR   SMR; Q6NHH1; -.
DR   STRING; 257309.DIP1166; -.
DR   DNASU; 2648566; -.
DR   EnsemblBacteria; CAE49686; CAE49686; DIP1166.
DR   KEGG; cdi:DIP1166; -.
DR   HOGENOM; CLU_016891_0_0_11; -.
DR   OMA; ISYNWLK; -.
DR   OrthoDB; 53568at2; -.
DR   Proteomes; UP000002198; 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: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; 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..836
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_0000126873"
FT   DOMAIN          44..160
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          420..495
FT                   /note="B5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          742..835
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         473
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         479
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         482
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         483
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   836 AA;  89783 MW;  1E0EF6FDA17AB650 CRC64;
     MLISQNWVTE LLGRSNPDWK VSPAELDSGY VRVGFETEGY SAIPETTGPL VIGRVETIEE
     LEGFKKPIRH CFVNVGDANG TGELQSIVCG ARNFQEGSYV VVSLPGAVLP GNFAISARET
     YGRMSAGMIC SAAELGLSDK QNSGIITLPN EIAEPGTDAR SIVGLDDTVF DVNITPDRGY
     ALSARGLTRE LASAFNLKFV DPAVDLNVAG VDTSDVPESS GELIKVDLRP ETQARRFGVR
     KVSGIDPKAP TPFWMQRELM LSGQRCVNAA TDVTNFVMLL LGQPMHAFDA NLIKGGLVVR
     NALEGESFET LDHVKRTLSA EDVVISDDTG IQSLAGVMGG TTSEISDETT DVFFEAANWH
     PITTARTSRR HKLSTEASRR FERGVDPEII EVALDVACAL LVSIAGGSVE SARTLIGSAP
     SMPQIRMKTS RPAELAGVAY SDATVIARLK EVGCAVEVDG DDLLVTPPTW RPDMTMSADL
     VEEVLRLEGL EDIPTIVPLA PVGSGLSPAQ LRRRAIGHAL AYSGYAEILP TPFIRNDTFD
     VWGLAADDER RSVVTVQNPL DAEYGVLATT LLPSMLEAVT RNVSRGQTSV NLFGLQQVSF
     KRGSGISPML DVRQRPSDNE VAELLNSLPV QPLHVATVGA GFMELEGPWG HGRTYSFADA
     IESARVVARA AGVELNVENV EMLPWHPGRC AALKAGDHIV GYAGELHPQI VEALNLPART
     CAMELDVSAL PLKESFPAPV LSAFPVLHQD LALVVDESVP AESVRKVIED AAGELLEKVE
     LFDVYRSEAL GAEKKSLAFS LEFRAQDRTL TDDECSEGRL AAAGRAAELF GATMRA
 
 
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