SYFB_UREPA
ID SYFB_UREPA Reviewed; 772 AA.
AC Q9PQ33;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=UU457;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
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; AF222894; AAF30869.1; -; Genomic_DNA.
DR RefSeq; WP_010891780.1; NC_002162.1.
DR AlphaFoldDB; Q9PQ33; -.
DR SMR; Q9PQ33; -.
DR STRING; 273119.UU457; -.
DR EnsemblBacteria; AAF30869; AAF30869; UU457.
DR GeneID; 29672674; -.
DR KEGG; uur:UU457; -.
DR PATRIC; fig|273119.6.peg.473; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR HOGENOM; CLU_016891_2_0_14; -.
DR OMA; ISYNWLK; -.
DR Proteomes; UP000000423; 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; 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; IPR005121; Fdx_antiC-bd.
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; 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; 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;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..772
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126980"
FT DOMAIN 40..158
FT /note="tRNA-binding"
FT DOMAIN 397..468
FT /note="B5"
FT DOMAIN 691..772
FT /note="FDX-ACB"
FT BINDING 446
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
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 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
SQ SEQUENCE 772 AA; 88192 MW; CCBE070438AEB6E6 CRC64;
MILSLNLLHK ISPKLKKIPL NELCAALMDL GCEVETINSI KPSTNLVFAK VLEKTRHPNA
NHLNLVKVKA NQKVYEIVCG ANNFSVHNWV VLAKLNAELA NGLKITPREL RGYVSNGMLC
AYSEINPQAT SFLTSTDLDG ILVLDDNYDH YKTPNQIFNL DDVILDLSIP SNRNDLNGYF
WIAKELCAYF DFEYVVDATI NHRPHKEIID VRILSDDVNS YGIIEVKNIQ NYILKWNTKS
ILINNQIKVL NNFADNMNFL TLLTANPLHA FDARKISGQI VVKNAEEDAI LLGLDQKEYL
IKKGDLIIVD DQKILALAGI IGSNDSKIDA TSTTAYIECA NFNPMLIANT ARRLKINTAA
AMRFSKPLTN YVTKVTLKKL LANFKSDAKL IYYFKHSVHN VIKNKINQVS DFVGAEIDLD
TAQTFLKRLG YKINKSNLIT PSHRYDVLNE FDVYEDIMKK ISIQEIKPQP ISFDILNFEN
NLAYDFEKKV SDFLVDQGLF ECKTYNLKNQ TQAHEFNFFN FKQAYEINNP TSNMRSHLKL
NNLNSLLEVL EYNQNQKNEL ENIFEISKIN PVDSSQQTVL SIILCKPLIN SKINDSLIVN
NFVTTKALLH ALLTKLNIDY AYDKNHVVNE LYDNNQLALI NANKQVFGFI GQLKNQVKKT
YGLSNDIFII NLNLTSYLNQ KQVITKVIKP SMYHDVIRDI SVKLASDVDL NNIIANIKKI
KNIRKVEISD LYIKDDGIIY TFKYYINDHL SNLSSEQIII IEQEVNNYLK QF
