SYFB_THET8
ID SYFB_THET8 Reviewed; 785 AA.
AC Q5SGX1;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, 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=TTHA1959;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1451792; DOI=10.1016/0014-5793(92)80215-3;
RA Keller B., Kast P., Hennecke H.;
RT "Cloning and sequence analysis of the phenylalanyl-tRNA synthetase genes
RT (pheST) from Thermus thermophilus.";
RL FEBS Lett. 301:83-88(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1508711; DOI=10.1093/nar/20.16.4173;
RA Kreutzer R., Kruft V., Bobkova E.V., Lavrik O.J., Sprinzl M.;
RT "Structure of the phenylalanyl-tRNA synthetase genes from Thermus
RT thermophilus HB8 and their expression in Escherichia coli.";
RL Nucleic Acids Res. 20:4173-4178(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9600851; DOI=10.1006/jmbi.1998.1744;
RA Lechler A., Kreutzer R.;
RT "The phenylalanyl-tRNA synthetase specifically binds DNA.";
RL J. Mol. Biol. 278:897-901(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=8199244; DOI=10.1016/0300-9084(93)90008-g;
RA Mosyak L., Safro M.;
RT "Phenylalanyl-tRNA synthetase from Thermus thermophilus has four
RT antiparallel folds of which only two are catalytically functional.";
RL Biochimie 75:1091-1098(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=7664121; DOI=10.1038/nsb0795-537;
RA Mosyak L., Reshetnikova L., Goldgur Y., Delarue M., Safro M.G.;
RT "Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus.";
RL Nat. Struct. Biol. 2:537-547(1995).
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}.
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DR EMBL; Z12118; CAA78105.1; -; Genomic_DNA.
DR EMBL; X65609; CAA46560.1; -; Genomic_DNA.
DR EMBL; Y15464; CAA75645.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71782.1; -; Genomic_DNA.
DR PIR; S22367; S22367.
DR PIR; T52503; T52503.
DR RefSeq; WP_011229047.1; NC_006461.1.
DR RefSeq; YP_145225.1; NC_006461.1.
DR PDB; 1EIY; X-ray; 3.30 A; B=1-785.
DR PDB; 1JJC; X-ray; 2.60 A; B=1-785.
DR PDB; 1PYS; X-ray; 2.90 A; B=1-785.
DR PDB; 3HFZ; X-ray; 2.90 A; B=1-785.
DR PDBsum; 1EIY; -.
DR PDBsum; 1JJC; -.
DR PDBsum; 1PYS; -.
DR PDBsum; 3HFZ; -.
DR AlphaFoldDB; Q5SGX1; -.
DR SMR; Q5SGX1; -.
DR STRING; 300852.55773341; -.
DR EnsemblBacteria; BAD71782; BAD71782; BAD71782.
DR GeneID; 3169713; -.
DR KEGG; ttj:TTHA1959; -.
DR PATRIC; fig|300852.9.peg.1931; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR HOGENOM; CLU_016891_0_0_0; -.
DR OMA; ISYNWLK; -.
DR PhylomeDB; Q5SGX1; -.
DR BRENDA; 6.1.1.20; 2305.
DR EvolutionaryTrace; Q5SGX1; -.
DR Proteomes; UP000000532; 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; 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;
KW Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..785
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126977"
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 CONFLICT 369..370
FT /note="QV -> AG (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 372..376
FT /note="AQRRA -> RPEAG (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 378..382
FT /note="SLLQA -> KPPPG (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:1JJC"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 62..76
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1EIY"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1PYS"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3HFZ"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:1JJC"
FT TURN 120..124
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1EIY"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:1JJC"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1JJC"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:1PYS"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1JJC"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:1EIY"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:1JJC"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 340..349
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:1JJC"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:3HFZ"
FT HELIX 369..384
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 408..415
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 421..430
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 438..445
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 456..467
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:1JJC"
FT TURN 486..489
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 490..505
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:3HFZ"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 549..562
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 566..592
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 605..620
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 624..628
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 634..655
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 657..662
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 669..676
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 693..697
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 700..705
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 707..718
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 722..731
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 740..749
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:1JJC"
FT HELIX 758..773
FT /evidence="ECO:0007829|PDB:1JJC"
FT TURN 774..776
FT /evidence="ECO:0007829|PDB:1JJC"
FT STRAND 778..784
FT /evidence="ECO:0007829|PDB:1PYS"
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
