ID   SYFB_NEIMB              Reviewed;         787 AA.
AC   Q9K089;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 129.
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=NMB0728;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF41141.1; -; Genomic_DNA.
DR   PIR; C81166; C81166.
DR   RefSeq; NP_273770.1; NC_003112.2.
DR   RefSeq; WP_002225459.1; NC_003112.2.
DR   AlphaFoldDB; Q9K089; -.
DR   SMR; Q9K089; -.
DR   STRING; 122586.NMB0728; -.
DR   PaxDb; Q9K089; -.
DR   EnsemblBacteria; AAF41141; AAF41141; NMB0728.
DR   KEGG; nme:NMB0728; -.
DR   PATRIC; fig|122586.8.peg.926; -.
DR   HOGENOM; CLU_016891_0_0_4; -.
DR   OMA; ISYNWLK; -.
DR   Proteomes; UP000000425; 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..787
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_0000126919"
FT   DOMAIN          39..149
FT                   /note="tRNA-binding"
FT   DOMAIN          400..475
FT                   /note="B5"
FT   DOMAIN          694..786
FT                   /note="FDX-ACB"
FT   BINDING         453
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
FT   BINDING         459
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
FT   BINDING         462
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"
SQ   SEQUENCE   787 AA;  86049 MW;  79CD0310861A366F CRC64;
     MQFSYSWLKT QADTELSSDK LEHLLTMSGL EVEEAETAAP AFAGVVIAEV KSVEKHPDAD
     RLNVTRVDAG TGGLVQIVCG APNVKAGIKV PCSLPGAVLP GNFKIKPTKM RGEVSDGMLC
     STDELGLPDD GVNGLHILPE DAPVGTNIRE YLDLDDTLFT LKITPNRADC LSIKGIAREV
     SALTGCAFRQ PEIHTAPITG SRKQPVQINA PADCGRFISR VIENVNARAT TPDWMKQRLE
     RSGIRSISAL VDIGNYVMLE IGQPMHVFDA DKLSGSLHIR RAREGETLEC LNEKTVSLSE
     NTLVVADEKG VLSLAGLMGG AASAVSDGTQ NIVLEAAWFA PEIIAGKSRQ YGFGSDSSFR
     FERGVDYRLQ ADAIERATEL VLQICGGAAG EMVEAQGELP EAKQVGLRLD RLKTVLGVDI
     PAEQVETILQ HLGLQPEKTA EGFRVTAPSF RFDIEIEADL IEEIGRVYGY ENIPDDYTSG
     RLKMLELPET RRPRFAVYNE MAARGYREVV SYAFVDEQWE QDFAANADPI RLQNPLAAQY
     AVMRSTLIGG LVEILQNNLN RKQNRVCVFE IARVFSKGSD GQFVQNERIG GLWYGAVMPE
     QWGGKTRNAD FYDIKADVEN LLKNKAVEFV KTGHPALHPG RAANIVSDGK VIGFVGELHP
     KWLQKYDLPQ APLVFEIDMA AVLECGKTRY RVVSKFQPVR RDLAFVMPEA MSHDDLLLVL
     KGAANKLVQE ISVFDVYRGT GLPEGMKSVA VKVILQDMEN TLTDEAVEPL IGKLIGAATA
     AGARLRS