SYFB_THETH
ID SYFB_THETH Reviewed; 785 AA.
AC P27002;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 151.
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;
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=10092459; DOI=10.1006/jmbi.1999.2617;
RA Reshetnikova L., Moor N., Lavrik O., Vassylyev D.G.;
RT "Crystal structures of phenylalanyl-tRNA synthetase complexed with
RT phenylalanine and a phenylalanyl-adenylate analogue.";
RL J. Mol. Biol. 287:555-568(1999).
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;
CC Note=Binds 2 magnesium ions per tetramer.;
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000305}.
CC -!- CAUTION: The sequence shown here has been extracted from PDB entry
CC 1B70. {ECO:0000305}.
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DR RefSeq; WP_011229047.1; NC_006461.1.
DR PDB; 1B70; X-ray; 2.70 A; B=1-785.
DR PDB; 1B7Y; X-ray; 2.50 A; B=1-785.
DR PDB; 2AKW; X-ray; 2.80 A; B=1-785.
DR PDB; 2ALY; X-ray; 2.60 A; B=1-785.
DR PDB; 2AMC; X-ray; 2.70 A; B=1-785.
DR PDB; 2IY5; X-ray; 3.10 A; B=1-785.
DR PDB; 3TEH; X-ray; 2.85 A; B=1-785.
DR PDB; 4TVA; X-ray; 2.60 A; B=1-785.
DR PDBsum; 1B70; -.
DR PDBsum; 1B7Y; -.
DR PDBsum; 2AKW; -.
DR PDBsum; 2ALY; -.
DR PDBsum; 2AMC; -.
DR PDBsum; 2IY5; -.
DR PDBsum; 3TEH; -.
DR PDBsum; 4TVA; -.
DR AlphaFoldDB; P27002; -.
DR SMR; P27002; -.
DR DIP; DIP-6105N; -.
DR MINT; P27002; -.
DR GeneID; 3169713; -.
DR EvolutionaryTrace; P27002; -.
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; 2.
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 RNA-binding; tRNA-binding.
FT CHAIN 1..785
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126978"
FT DOMAIN 39..147
FT /note="tRNA-binding"
FT DOMAIN 399..474
FT /note="B5"
FT DOMAIN 688..780
FT /note="FDX-ACB"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:1B7Y"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:1B7Y"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:1B70"
FT STRAND 62..76
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3TEH"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3TEH"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:1B7Y"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:1B7Y"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:1B7Y"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 340..349
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 369..383
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 408..415
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 421..430
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 434..445
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 456..467
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:1B7Y"
FT TURN 486..489
FT /evidence="ECO:0007829|PDB:3TEH"
FT HELIX 490..505
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 549..562
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 568..592
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 606..620
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 634..644
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 647..655
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 657..662
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 669..676
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 693..697
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 701..705
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 707..718
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 722..729
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 737..739
FT /evidence="ECO:0007829|PDB:3TEH"
FT STRAND 744..749
FT /evidence="ECO:0007829|PDB:1B7Y"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:1B7Y"
FT HELIX 758..773
FT /evidence="ECO:0007829|PDB:1B7Y"
FT TURN 774..776
FT /evidence="ECO:0007829|PDB:3TEH"
SQ SEQUENCE 785 AA; 86611 MW; BDC51952DE8E0F00 CRC64;
MRVPFSWLKA YVPELESPEV LEERLAGLGF ETDRIERVFP IPRGVVFARV LEAHPIPGTR
LKRLVLDAGR TVEVVSGAEN ARKGIGVALA LPGTELPGLG QKVGERVIQG VRSFGMALSP
RELGVGEYGG GLLEFPEDAL PPGTPLSEAW PEEVVLDLEV TPNRPDALGL LGLARDLHAL
GYALVEPEAA LKAEALPLPF ALKVEDPEGA PHFTLGYAFG LRVAPSPLWM QRALFAAGMR
PINNVVDVTN YVMLERAQPM HAFDLRFVGE GIAVRRAREG ERLKTLDGVE RTLHPEDLVI
AGWRGEESFP LGLAGVMGGA ESEVREDTEA IALEVACFDP VSIRKTARRH GLRTEASHRF
ERGVDPLGQV PAQRRALSLL QALAGARVAE ALLEAGSPKP PEAIPFRPEY ANRLLGTSYP
EAEQIAILKR LGCRVEGEGP TYRVTPPSHR LDLRLEEDLV EEVARIQGYE TIPLALPAFF
PAPDNRGVEA PYRKEQRLRE VLSGLGFQEV YTYSFMDPED ARRFRLDPPR LLLLNPLAPE
KAALRTHLFP GLVRVLKENL DLDRPERALL FEVGRVFRER EETHLAGLLF GEGVGLPWAK
ERLSGYFLLK GYLEALFARL GLAFRVEAQA FPFLHPGVSG RVLVEGEEVG FLGALHPEIA
QELELPPVHL FELRLPLPDK PLAFQDPSRH PAAFRDLAVV VPAPTPYGEV EALVREAAGP
YLESLALFDL YQGPPLPEGH KSLAFHLRFR HPKRTLRDEE VEEAVSRVAE ALRARGFGLR
GLDTP
