ID   SYFB_SYNY3              Reviewed;         810 AA.
AC   P74296;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 149.
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=sll1553;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA18390.1; -; Genomic_DNA.
DR   PIR; S75931; S75931.
DR   AlphaFoldDB; P74296; -.
DR   SMR; P74296; -.
DR   IntAct; P74296; 4.
DR   STRING; 1148.gene:10499266; -.
DR   PaxDb; 1148-1653476; -.
DR   EnsemblBacteria; BAA18390; BAA18390; BAA18390.
DR   KEGG; syn:sll1553; -.
DR   eggNOG; COG0072; Bacteria.
DR   eggNOG; COG0073; Bacteria.
DR   InParanoid; P74296; -.
DR   PhylomeDB; P74296; -.
DR   Proteomes; UP000001425; 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; 3.30.56.10; -; 2.
DR   Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 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   NCBIfam; TIGR00472; pheT_bact; 1.
DR   PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1.
DR   PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 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; SSF54991; Anticodon-binding domain of PheRS; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF56037; PheT/TilS domain; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 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..810
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_0000126974"
FT   DOMAIN          39..150
FT                   /note="tRNA-binding"
FT   DOMAIN          407..495
FT                   /note="B5"
FT   DOMAIN          716..809
FT                   /note="FDX-ACB"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
FT   BINDING         479
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
FT   BINDING         482
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
FT   BINDING         483
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   810 AA;  87888 MW;  4D14168774C12BE9 CRC64;
     MRISVNWLQS LVELNLSPEE LGELLTIAGL EVEEIEDRRS WAAGVVLGRV ISREKHPNAD
     KLSVCVVDIG TEEPSTIVCG AANVRADILV PVATLGSYLP KVDLKIKPAK LRGVKSSGMI
     CSLAELGLSK ESEGIHIFPD LDLPSGSPVG PLLGLDDVIL EISPTANRAD ALSMVGVARE
     VAALTGGKLS LPEIKAVSVS DQDLPISVTE PQACPTYVGT VIRGVKVGPS PDWLQQRLLA
     AGTRPINNVV DVTNYVLLEW GQPLHSFDQD KLQTLVGPEG FALGVRFAEE GEKLITLDDQ
     ERTLQPQNLL VTANDQPVAI AGVMGGAATE VDENTQNIVL ETALFDGVTI RKSSKAINLR
     SESSTRYERG VNRCELEVAL HRAIALMTEL AGGTVVRQGK ADQRQDRGEA IINLRLERLQ
     QLLGKVNTPT GIGNITAEDV ERILTDLGCG LTRQSDSDTP VWAVTVPSYR QRDIEREIDL
     IEEVARLYGY DHFCEQLPSN TIAGGLSPSY QAELALREAC RGVGLTEVVH YSLVKPHGSE
     VMLANPLFAE YSALRTNLLD GLITAFANNQ AQNNGALNAF EVGRVFWQNE GDIGEADHLA
     GICGGSQITE GTWPQGGKPQ PMSWYDAKGL LEAIFQRLGA TVTYSGDHQD PRLHPGRTAL
     LSCNGTVLGR FGQLHPQLRR EKGLIDEVYA FEITLTPLYQ AMETQILGTP DFRPYSPYPA
     VARDLALYAP LELTVAELTQ AMVKAGGDLL EQVELFDEYR GQSVPAGQRS LAFSLAYRVG
     DRTLTDADVE PLHNQIREAL TKQFAVSLRS
//