SYFB_BUCAP
ID SYFB_BUCAP Reviewed; 798 AA.
AC P59057;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=BUsg_122;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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}.
CC -!- CAUTION: Lacks the conserved glutamate residue in position 464 that
CC binds magnesium; it is replaced by a glycine residue. {ECO:0000305}.
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DR EMBL; AE013218; AAM67690.1; -; Genomic_DNA.
DR RefSeq; WP_011053657.1; NC_004061.1.
DR AlphaFoldDB; P59057; -.
DR SMR; P59057; -.
DR STRING; 198804.BUsg_122; -.
DR EnsemblBacteria; AAM67690; AAM67690; BUsg_122.
DR KEGG; bas:BUsg_122; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR HOGENOM; CLU_016891_0_0_6; -.
DR OMA; ISYNWLK; -.
DR OrthoDB; 53568at2; -.
DR Proteomes; UP000000416; 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..798
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126857"
FT DOMAIN 39..148
FT /note="tRNA-binding"
FT DOMAIN 402..477
FT /note="B5"
FT DOMAIN 704..797
FT /note="FDX-ACB"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
SQ SEQUENCE 798 AA; 92418 MW; 70D3A550999237DB CRC64;
MKFNENWLRE WINPKITSVS LRNQIVESGI EIESIHEFNP IFDGFLVGKI VECINPCKGN
NLKILKVDVG YKKLLNIVCG ASNCRNNIKV VVATIDSILP NGSKIKIKKI KEKLSEGMIC
SFFELGLFNF CKDIIELPED IPIGKKINDL FLLKKDTFIK VAVTPNRPDG LSILGIARNI
AAINNLKKIR LKKRILPTTI EDQFPITINT EKQSVNYFGR IIQNVNLNVD TPFWMKKKLF
FCDLLSDNII ENILNYILIE IGQPLNILNA DKIDDVIEIR MAIKKEFLIL KNDTRIVLDK
DILVFSDKTK ILFIPGNINN SDLEPNKNTK NIFLTSYLVD KKSILNILKK IDSNNILDYY
SHGVDASLQK YAIEYATYLI VKICGGKIGP INTKKSNFNS LSCSNKIKLY HQNFNKCIDS
FVDSSIISNI LLCLEYKVNF HKKYWYVFPP SWRFDILIEE DVIGDILRIY NYNNIPLTPL
KQNYYFNSKN KDLKSPLLDE AAVLLINRGY YEIITYSFIN PSLQDDIIPN NNQILISNPI
SKDFSSMRLS LWPGLLKTVS YNKNRQQESM RFFERGLCFS IDESQILGIR QEMFLGGVIS
GFYSKENWFS VRRKVDFYDL KGDLESLLEV ICGLNKFEIR HQNILGLHPE QSAKIYLDNK
YIGSLGKIHP KIEKKLNLYN STFLFELSLN YISKLKFYNT EEISKYPTSR RDIAILVSKD
IPFLDIITVC KDFFVNKKVE INLFDVYSCK EFDNRKKSLG ISFVFQNFKK NLKENEVNLM
LHDCIKILKK KFQVVLRK
