SYFB_SALTY
ID SYFB_SALTY Reviewed; 795 AA.
AC P15434; O30910;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 3.
DT 03-AUG-2022, entry version 153.
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=STM1338;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 525-674.
RX PubMed=9302299; DOI=10.1126/science.277.5334.2007;
RA Valdivia R.H., Falkow S.;
RT "Fluorescence-based isolation of bacterial genes expressed within host
RT cells.";
RL Science 277:2007-2011(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 779-795.
RC STRAIN=LT2;
RX PubMed=2685752; DOI=10.1093/nar/17.21.8880;
RA Li Z.J., Hillyard D., Higgins P.;
RT "Nucleotide sequence of the Salmonella typhimurium himA gene.";
RL Nucleic Acids Res. 17:8880-8880(1989).
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; AE006468; AAL20263.1; -; Genomic_DNA.
DR EMBL; AF020811; AAB80744.1; -; Genomic_DNA.
DR EMBL; X16739; CAA34712.1; -; Genomic_DNA.
DR PIR; S09607; S09607.
DR RefSeq; NP_460304.1; NC_003197.2.
DR RefSeq; WP_000672402.1; NC_003197.2.
DR AlphaFoldDB; P15434; -.
DR SMR; P15434; -.
DR STRING; 99287.STM1338; -.
DR PaxDb; P15434; -.
DR EnsemblBacteria; AAL20263; AAL20263; STM1338.
DR GeneID; 1252856; -.
DR KEGG; stm:STM1338; -.
DR PATRIC; fig|99287.12.peg.1421; -.
DR HOGENOM; CLU_016891_0_0_6; -.
DR OMA; ISYNWLK; -.
DR PhylomeDB; P15434; -.
DR BioCyc; SENT99287:STM1338-MON; -.
DR Proteomes; UP000001014; 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; 3.30.70.380; -; 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 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..795
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126944"
FT DOMAIN 39..148
FT /note="tRNA-binding"
FT DOMAIN 401..476
FT /note="B5"
FT DOMAIN 701..794
FT /note="FDX-ACB"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT CONFLICT 608
FT /note="A -> P (in Ref. 2; AAB80744)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="L -> M (in Ref. 2; AAB80744)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="G -> A (in Ref. 2; AAB80744)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="I -> N (in Ref. 2; AAB80744)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 795 AA; 87253 MW; B1F937A861979CE4 CRC64;
MKFSELWLRE WVNPAIDSDA LANQITMAGL EVDGVEPVAG SFNGVVVGEV VECAQHPNAD
KLRVTKVNVG GERLLDIVCG APNCRQGLKV AVATIGAILP GDFKIKAAKL RGEPSEGMLC
SFSELGISDD HSGIIELPAD APLGTDIREY LKLDDNTIEI SVTPNRADCL GIIGVARDVA
VLNKAPLQEP EMAPVTATIS DTLPITVEAA DACPRYLGRV VKGINVNAPT PLWMKEKLRR
CGIRSIDAVV DVTNYVLLEL GQPMHAFDKD RIDGGIVVRM AKEGETVVLL DGSEATLNAD
TLVIADHHKA LGIAGIFGGE HSGVNGETQN VLLECAYFNP LSITGRARRH GLHTDASHRY
ERGVDPALQY KAIERATRLL LDICGGDAGP IIDVSNEATL PKRATITLRR SKLDRLIGHH
IADEQVSDIL RRLGCEVTEG QDEWKAVAPT WRFDMEIEED LVEEVARVYG YNNIPDEPIQ
AGLIMGTHRE ADLSLKRVKT MLNDKGYQEV ITYSFVDPKV QQLIHPGAEA LLLPNPISVE
MSAMRLSLWS GLLATVVYNQ NRQQNRVRIF ETGLRFVPDT QANLGIRQDL MLAGVICGNR
YDEHWNLAKE TVDFYDLKGD LEAVLDLTGK LGDIQFKAEM NPALHPGQSA AIYLKDERIG
FIGVVHPELE RKLDLNGRTL VFELEWNKLA DRIVPQAREI SRFPANRRDI AVVVAENVPA
ADILSECKKV GVNQVVGVNL FDVYRGKGVA EGYKSLAISL ILQDTNRTLE EEEIAATVAK
CVEALKERFQ ASLRD
