SYFB_BACFN
ID SYFB_BACFN Reviewed; 820 AA.
AC Q5LC76;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=BF2590;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
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; CR626927; CAH08290.1; -; Genomic_DNA.
DR RefSeq; WP_005788108.1; NC_003228.3.
DR PDB; 3IG2; X-ray; 2.09 A; A/B/C/D=504-713.
DR PDBsum; 3IG2; -.
DR AlphaFoldDB; Q5LC76; -.
DR SMR; Q5LC76; -.
DR STRING; 272559.BF9343_2509; -.
DR PRIDE; Q5LC76; -.
DR DNASU; 3287358; -.
DR EnsemblBacteria; CAH08290; CAH08290; BF9343_2509.
DR KEGG; bfs:BF9343_2509; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR HOGENOM; CLU_016891_0_0_10; -.
DR OMA; ISYNWLK; -.
DR OrthoDB; 53568at2; -.
DR EvolutionaryTrace; Q5LC76; -.
DR Proteomes; UP000006731; 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..820
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000232046"
FT DOMAIN 42..154
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT DOMAIN 413..489
FT /note="B5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT DOMAIN 727..820
FT /note="FDX-ACB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT BINDING 467
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 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 476
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 477
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 HELIX 505..519
FT /evidence="ECO:0007829|PDB:3IG2"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:3IG2"
FT HELIX 533..536
FT /evidence="ECO:0007829|PDB:3IG2"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:3IG2"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:3IG2"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:3IG2"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:3IG2"
FT HELIX 566..575
FT /evidence="ECO:0007829|PDB:3IG2"
FT STRAND 579..582
FT /evidence="ECO:0007829|PDB:3IG2"
FT STRAND 585..595
FT /evidence="ECO:0007829|PDB:3IG2"
FT STRAND 609..623
FT /evidence="ECO:0007829|PDB:3IG2"
FT HELIX 634..650
FT /evidence="ECO:0007829|PDB:3IG2"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:3IG2"
FT STRAND 659..663
FT /evidence="ECO:0007829|PDB:3IG2"
FT STRAND 665..675
FT /evidence="ECO:0007829|PDB:3IG2"
FT STRAND 681..688
FT /evidence="ECO:0007829|PDB:3IG2"
FT HELIX 690..695
FT /evidence="ECO:0007829|PDB:3IG2"
FT STRAND 700..708
FT /evidence="ECO:0007829|PDB:3IG2"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:3IG2"
SQ SEQUENCE 820 AA; 90708 MW; 625EDDA619D8A630 CRC64;
MNISYNWLKE YVNFDLTPDE VAAALTSIGL ETGGVEEVQT IKGGLEGLVI GEVLTCVEHP
NSDHLHITTV NLGNGEPTQI VCGAPNVAAG QKVVVATLGT KLYDGDECFT IKKSKIRGVE
SIGMICAEDE IGIGTSHDGI IVLPEDAVPG TLAKDYYNVK SDYVLEVDIT PNRADACSHY
GVARDLYAYL VQNGKQAALT RPSVDAFAVE NHDLDIKVTV ENSEACPRYA GVTVKGVTVK
ESPEWLQNKL RIIGLRPINN VVDITNYIVH AFGQPLHCFD ANKIKGGEVI VKTMPEGTTF
VTLDGVERKL NERDLMICNK EDAMCIAGVF GGLDSGSTEA TTDVFLESAY FHPTWVRKTA
RRHGLNTDAS FRFERGIDPN ITIYCLKLAA MMVKELAGGT ISSEIKDVCA APAQDFIVEL
TYEKVHSLIG KVIPVETIKS IVTSLEMKIM DETAEGLTLA VPPYRVDVQR DCDVIEDILR
IYGYNNVEIP STLKSSLTTK GDCDKSNKLQ NLVAEQLVGC GFNEILNNSL TRAAYYDGLE
SYPSKNLVML LNPLSADLNC MRQTLLFGGL ESIAHNANRK NADLKFFEFG NCYHFDAEKK
NPEKVLAPYS EDYHLGLWVT GKMVSNSWAH ADENTSVYEL KAYVENIFKR LGLDLHSLVV
GNLSDDIYST ALTVNTKGGK RLATFGVVTK KMLKAFDVDN EVYYADLNWK ELMKAIRSVK
VSYKEISKFP AVKRDLALLL DKKVQFAEIE KIAYETEKKL LKEVSLFDVY EGKNLEAGKK
SYAVSFLLQD ESQTLNDKMI DKIMSKLVKN LEDKLGAKLR
