SYFB_MYCGE
ID SYFB_MYCGE Reviewed; 806 AA.
AC P47437; Q49516;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=MG195;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94 AND 682-798.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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; L43967; AAC71413.1; -; Genomic_DNA.
DR EMBL; U01711; AAB01024.1; -; Genomic_DNA.
DR EMBL; U02173; AAD12455.1; -; Genomic_DNA.
DR PIR; E64221; E64221.
DR RefSeq; WP_009885736.1; NZ_AAGX01000004.1.
DR AlphaFoldDB; P47437; -.
DR SMR; P47437; -.
DR STRING; 243273.MG_195; -.
DR PRIDE; P47437; -.
DR EnsemblBacteria; AAC71413; AAC71413; MG_195.
DR KEGG; mge:MG_195; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR HOGENOM; CLU_016891_2_0_14; -.
DR OMA; ISYNWLK; -.
DR OrthoDB; 53568at2; -.
DR BioCyc; MGEN243273:G1GJ2-227-MON; -.
DR Proteomes; UP000000807; 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; 3.30.930.10; -; 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; 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; PF01588; tRNA_bind; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00472; pheT_bact; 1.
DR PROSITE; PS51483; B5; 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..806
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126912"
FT DOMAIN 40..153
FT /note="tRNA-binding"
FT DOMAIN 413..487
FT /note="B5"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT CONFLICT 81..94
FT /note="NANNINNPDNINKF -> MLITLTILYIHSCL (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 806 AA; 92133 MW; D2F2BA6E9A064478 CRC64;
MLISKKTLGV LIPDIFSFSN DQIAQKLEQM GIEVESIKQF NSPDYLQLAK VVSIQPHPHD
NKLFICELQI DKNKFINVVS NANNINNPDN INKFVIVAKK GTELLNGLIV KTQNIKGIIS
EGILCSYIDI NPFSRQIIEK TEVADAIIID HVSNDHDWNQ YLSFLSLDDV IFDVKTPTNR
ADLHSLIFLA KELGVLLKTK TFLKQKSSVV NHDFFKFPLN LKNKLKANYF GGLFLRQINQ
HSSPWTVKGL LINQMIKPVN YYVDKANLVT VFTAQPIHCH DADRIVGNIE LKQATHNETF
VGLDDKQYEI EPGDIVVCDE KGIIALVGII GSKRTMVQPT TTNIFFEVVN CNSETIKQTA
KRFLINNFAS KFMVKPISLL ATDNCLNYLQ NSLLTTDNIG KISHFSSSLK VEPFSKKLTV
NFHKIRQLIG IEKKELTDQT IKKSLSQLGF KVDNQLLKIP SYRQDINTWQ DISEEIVKLI
DINKLKPIGI TSSFNFEKSS YFNTFNALTK LRKKLQTLGF HNVITYQLTD QKSAKTFNLF
NLENFITIKN PVSQNHSVMR VSLIDSLLKV LKTNNNYKNE LVNIFEFSFI KTQNNSELHL
AVLWVEKLFT SSFNPMQGIS NDVFTMKGLA KLIVANLGFS CDFEPLDDSD YFVNNQSLKI
VVFNEQIGFI GLIKESLLNN YDLNNKPIYC LEINLDRMLS SLNRIEKNYL GYSKLQPVCK
DLTFSFTNPA SHFDQFANMI KRITGIESWK LISVFETMQN NQLITKYTVR YFLKNDANKP
LTNQTIELIT NNLKLQCEKL KIKLDI
