ID   SYFB_PROM9              Reviewed;         814 AA.
AC   Q31AV5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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};
GN   OrderedLocusNames=PMT9312_0930;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000111; ABB49990.1; -; Genomic_DNA.
DR   RefSeq; WP_011376484.1; NC_007577.1.
DR   AlphaFoldDB; Q31AV5; -.
DR   SMR; Q31AV5; -.
DR   STRING; 74546.PMT9312_0930; -.
DR   PRIDE; Q31AV5; -.
DR   EnsemblBacteria; ABB49990; ABB49990; PMT9312_0930.
DR   KEGG; pmi:PMT9312_0930; -.
DR   eggNOG; COG0072; Bacteria.
DR   HOGENOM; CLU_016891_0_0_3; -.
DR   OMA; ISYNWLK; -.
DR   OrthoDB; 53568at2; -.
DR   Proteomes; UP000002715; 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; RNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..814
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_0000232074"
FT   DOMAIN          39..153
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          414..500
FT                   /note="B5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          720..813
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         478
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         484
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         487
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         488
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   814 AA;  91363 MW;  9A811FA3F93A7192 CRC64;
     MKVSQNWLKN LVEISSTPVD LSEKLSIGGF EVESLEDCSK NVNGVVLGKV LSVLKHDGSD
     KLSICQVDIG TSKNLQIICG ARNIKPNVYV YVATVGAKLN AVDLTIKRSE IRGVMSEGMI
     CSLQELGLED SSEGIEIIDE DLALKHELGT PVSDLLQLND FIYDLAITAN RPDGMSVIGI
     AREISALLES KLSFPELNHK YNIHLNKGIK LCPEAITSNC IYTISCIDGV NGNKLSPIWL
     KDRIEKSGIK SINLLVDLTN YILLEQGQPL HAFDKEKLSN LIGKDVSPED FSVRKAKDNE
     SLVCLDGKKY ELNENITVVT CSDKPVAIAG VIGGLETSVS NTTSSIYLEG AVFNPVTIRK
     SSKAVGIRTE SSSRYEKGIS SKNTISAVTR AMNLLEEYFS INLPIINTSN LKNNEDIFIK
     LRRSRIHKIL GPLIINDQFE KRNISDTEIV DKLTLIGCSL KSKEYGWDVA VIPNRSQDLI
     REIDLIEEIA RLIGYDRFDL NLPNPIKPGK LSSEQLALRK VKNGFTENGF NEVLSYSLVP
     EDKETLIKIS NPLLLETSCL RDNIWKEHLE IVNRNIKAGQ NSCYIFEIGN VFHKNTEFIQ
     KEVLNGAIFG NKRFEKWVNS NKDNDLNYYQ ARGKLKEALS SLNIKIDDKP TDSIDFLHPG
     RTAKLIIEGK DAGYFGEIHP KLILEKKSLK IVYLFSINVD NLLGASTRKN KWIPIFKQYP
     IVPKIERDIN FVFSKKFLIS DITSLIKKTG KNLLEDVYLI DIFEDIKLGE DYISYTFRLS
     YRAQDKTLLD SDIKTIHSSI ISNIEKSFQT KLRN