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P07395

- SYFB_ECOLI

UniProt

P07395 - SYFB_ECOLI

Protein

Phenylalanine--tRNA ligase beta subunit

Gene

pheT

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).

    Cofactori

    Binds 2 magnesium ions per tetramer.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi454 – 4541MagnesiumBy similarity
    Metal bindingi460 – 4601Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi463 – 4631MagnesiumBy similarity
    Metal bindingi464 – 4641MagnesiumBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. identical protein binding Source: IntAct
    3. magnesium ion binding Source: UniProtKB-HAMAP
    4. phenylalanine-tRNA ligase activity Source: UniProtKB-HAMAP
    5. protein binding Source: IntAct
    6. tRNA binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. phenylalanyl-tRNA aminoacylation Source: UniProtKB-HAMAP
    2. tRNA processing Source: InterPro

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PHET-MONOMER.
    ECOL316407:JW1703-MONOMER.
    MetaCyc:PHET-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenylalanine--tRNA ligase beta subunit (EC:6.1.1.20)
    Alternative name(s):
    Phenylalanyl-tRNA synthetase beta subunit
    Short name:
    PheRS
    Gene namesi
    Name:pheT
    Ordered Locus Names:b1713, JW1703
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10710. pheT.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 795795Phenylalanine--tRNA ligase beta subunitPRO_0000126880Add
    BLAST

    Proteomic databases

    PaxDbiP07395.
    PRIDEiP07395.

    2D gel databases

    SWISS-2DPAGEP07395.

    Expressioni

    Gene expression databases

    GenevestigatoriP07395.

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta subunits.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-555713,EBI-555713
    mdtOP327153EBI-555713,EBI-555775
    pheSP083127EBI-555713,EBI-555676
    secDP0AG903EBI-555713,EBI-555724

    Protein-protein interaction databases

    DIPiDIP-6879N.
    IntActiP07395. 12 interactions.
    MINTiMINT-1231494.
    STRINGi511145.b1713.

    Structurei

    Secondary structure

    1
    795
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 43
    Helixi5 – 95
    Helixi20 – 267
    Turni27 – 293
    Beta strandi31 – 399
    Beta strandi45 – 5410
    Beta strandi64 – 685
    Beta strandi70 – 734
    Beta strandi75 – 784
    Beta strandi89 – 935
    Beta strandi108 – 11912
    Helixi123 – 1253
    Helixi147 – 1504
    Beta strandi156 – 1616
    Helixi172 – 18312
    Turni210 – 2123
    Beta strandi214 – 22310
    Helixi233 – 2408
    Helixi249 – 26012
    Beta strandi264 – 2685
    Helixi269 – 2713
    Beta strandi277 – 2793
    Beta strandi287 – 2893
    Turni290 – 2923
    Beta strandi293 – 2953
    Beta strandi303 – 3053
    Beta strandi307 – 3137
    Turni314 – 3163
    Beta strandi331 – 3377
    Helixi340 – 3423
    Helixi346 – 3494
    Helixi355 – 3628
    Helixi369 – 38113
    Beta strandi387 – 3959
    Turni397 – 3993
    Beta strandi405 – 4095
    Helixi410 – 4178
    Helixi423 – 43311
    Beta strandi436 – 4405
    Beta strandi443 – 4475
    Helixi458 – 46912
    Helixi471 – 4733
    Beta strandi480 – 4823
    Helixi495 – 50410
    Beta strandi514 – 5163
    Helixi518 – 5247
    Beta strandi525 – 5273
    Beta strandi546 – 5483
    Helixi549 – 56012
    Beta strandi568 – 57811
    Beta strandi586 – 60116
    Beta strandi605 – 6073
    Helixi614 – 62411
    Turni625 – 6273
    Beta strandi644 – 6529
    Turni654 – 6563
    Beta strandi660 – 6656
    Turni667 – 6737
    Beta strandi679 – 6857
    Helixi686 – 6883
    Beta strandi689 – 6913
    Beta strandi706 – 71510
    Helixi720 – 7245
    Turni725 – 7273
    Turni730 – 7345
    Beta strandi735 – 7406
    Beta strandi753 – 76210
    Helixi771 – 78414
    Turni785 – 7895

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3PCOX-ray3.02B/D1-795[»]
    ProteinModelPortaliP07395.
    SMRiP07395. Positions 1-795.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 148110tRNA-bindingAdd
    BLAST
    Domaini401 – 47676B5Add
    BLAST
    Domaini701 – 79494FDX-ACBAdd
    BLAST

    Sequence similaritiesi

    Contains 1 B5 domain.Curated
    Contains 1 FDX-ACB domain.Curated
    Contains 1 tRNA-binding domain.Curated

    Phylogenomic databases

    eggNOGiCOG0073.
    HOGENOMiHOG000292085.
    KOiK01890.
    OMAiNYVMIEL.
    OrthoDBiEOG6CCH1J.
    PhylomeDBiP07395.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    3.30.56.20. 1 hit.
    3.30.70.380. 1 hit.
    3.50.40.10. 1 hit.
    HAMAPiMF_00283. Phe_tRNA_synth_beta1.
    InterProiIPR005146. B3/B4_tRNA-bd.
    IPR009061. DNA-bd_dom_put.
    IPR012340. NA-bd_OB-fold.
    IPR004532. Phe-tRNA-ligase_IIc_bsu.
    IPR020825. Phe-tRNA_synthase_B3/B4.
    IPR005121. PheS_beta_Fdx_antiC-bd.
    IPR002547. tRNA-bd_dom.
    IPR005147. tRNA_synthase_B5-dom.
    [Graphical view]
    PfamiPF03483. B3_4. 1 hit.
    PF03484. B5. 1 hit.
    PF03147. FDX-ACB. 1 hit.
    PF01588. tRNA_bind. 1 hit.
    [Graphical view]
    SMARTiSM00873. B3_4. 1 hit.
    SM00874. B5. 1 hit.
    SM00896. FDX-ACB. 1 hit.
    [Graphical view]
    SUPFAMiSSF46955. SSF46955. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF54991. SSF54991. 1 hit.
    SSF56037. SSF56037. 1 hit.
    TIGRFAMsiTIGR00472. pheT_bact. 1 hit.
    PROSITEiPS51483. B5. 1 hit.
    PS51447. FDX_ACB. 1 hit.
    PS50886. TRBD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P07395-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFSELWLRE WVNPAIDSDA LANQITMAGL EVDGVEPVAG SFHGVVVGEV    50
    VECAQHPNAD KLRVTKVNVG GDRLLDIVCG APNCRQGLRV AVATIGAVLP 100
    GDFKIKAAKL RGEPSEGMLC SFSELGISDD HSGIIELPAD APIGTDIREY 150
    LKLDDNTIEI SVTPNRADCL GIIGVARDVA VLNQLPLVQP EIVPVGATID 200
    DTLPITVEAP EACPRYLGRV VKGINVKAPT PLWMKEKLRR CGIRSIDAVV 250
    DVTNYVLLEL GQPMHAFDKD RIEGGIVVRM AKEGETLVLL DGTEAKLNAD 300
    TLVIADHNKA LAMGGIFGGE HSGVNDETQN VLLECAFFSP LSITGRARRH 350
    GLHTDASHRY ERGVDPALQH KAMERATRLL IDICGGEAGP VIDITNEATL 400
    PKRATITLRR SKLDRLIGHH IADEQVTDIL RRLGCEVTEG KDEWQAVAPS 450
    WRFDMEIEED LVEEVARVYG YNNIPDEPVQ ASLIMGTHRE ADLSLKRVKT 500
    LLNDKGYQEV ITYSFVDPKV QQMIHPGVEA LLLPSPISVE MSAMRLSLWT 550
    GLLATVVYNQ NRQQNRVRIF ESGLRFVPDT QAPLGIRQDL MLAGVICGNR 600
    YEEHWNLAKE TVDFYDLKGD LESVLDLTGK LNEVEFRAEA NPALHPGQSA 650
    AIYLKGERIG FVGVVHPELE RKLDLNGRTL VFELEWNKLA DRVVPQAREI 700
    SRFPANRRDI AVVVAENVPA ADILSECKKV GVNQVVGVNL FDVYRGKGVA 750
    EGYKSLAISL ILQDTSRTLE EEEIAATVAK CVEALKERFQ ASLRD 795
    Length:795
    Mass (Da):87,378
    Last modified:November 1, 1997 - v2
    Checksum:i3B55EC65D25937E5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti93 – 931A → T in CAA23565. (PubMed:2991205)Curated
    Sequence conflicti141 – 1422AP → VR in CAA23565. (PubMed:2991205)Curated
    Sequence conflicti186 – 1894PLVQ → AAGN in CAA23565. (PubMed:2991205)Curated
    Sequence conflicti481 – 4811A → R in CAA23565. (PubMed:2991205)Curated
    Sequence conflicti698 – 6981R → G in CAA23565. (PubMed:2991205)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00291 Genomic DNA. Translation: CAA23565.1.
    K02844 Genomic DNA. Translation: AAA51470.1.
    U00096 Genomic DNA. Translation: AAC74783.1.
    AP009048 Genomic DNA. Translation: BAA15481.1.
    PIRiI41284. SYECFB.
    RefSeqiNP_416228.1. NC_000913.3.
    YP_489975.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74783; AAC74783; b1713.
    BAA15481; BAA15481; BAA15481.
    GeneIDi12933094.
    945382.
    KEGGiecj:Y75_p1688.
    eco:b1713.
    PATRICi32118732. VBIEscCol129921_1784.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00291 Genomic DNA. Translation: CAA23565.1 .
    K02844 Genomic DNA. Translation: AAA51470.1 .
    U00096 Genomic DNA. Translation: AAC74783.1 .
    AP009048 Genomic DNA. Translation: BAA15481.1 .
    PIRi I41284. SYECFB.
    RefSeqi NP_416228.1. NC_000913.3.
    YP_489975.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3PCO X-ray 3.02 B/D 1-795 [» ]
    ProteinModelPortali P07395.
    SMRi P07395. Positions 1-795.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6879N.
    IntActi P07395. 12 interactions.
    MINTi MINT-1231494.
    STRINGi 511145.b1713.

    2D gel databases

    SWISS-2DPAGE P07395.

    Proteomic databases

    PaxDbi P07395.
    PRIDEi P07395.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74783 ; AAC74783 ; b1713 .
    BAA15481 ; BAA15481 ; BAA15481 .
    GeneIDi 12933094.
    945382.
    KEGGi ecj:Y75_p1688.
    eco:b1713.
    PATRICi 32118732. VBIEscCol129921_1784.

    Organism-specific databases

    EchoBASEi EB0704.
    EcoGenei EG10710. pheT.

    Phylogenomic databases

    eggNOGi COG0073.
    HOGENOMi HOG000292085.
    KOi K01890.
    OMAi NYVMIEL.
    OrthoDBi EOG6CCH1J.
    PhylomeDBi P07395.

    Enzyme and pathway databases

    BioCyci EcoCyc:PHET-MONOMER.
    ECOL316407:JW1703-MONOMER.
    MetaCyc:PHET-MONOMER.

    Miscellaneous databases

    PROi P07395.

    Gene expression databases

    Genevestigatori P07395.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    3.30.56.20. 1 hit.
    3.30.70.380. 1 hit.
    3.50.40.10. 1 hit.
    HAMAPi MF_00283. Phe_tRNA_synth_beta1.
    InterProi IPR005146. B3/B4_tRNA-bd.
    IPR009061. DNA-bd_dom_put.
    IPR012340. NA-bd_OB-fold.
    IPR004532. Phe-tRNA-ligase_IIc_bsu.
    IPR020825. Phe-tRNA_synthase_B3/B4.
    IPR005121. PheS_beta_Fdx_antiC-bd.
    IPR002547. tRNA-bd_dom.
    IPR005147. tRNA_synthase_B5-dom.
    [Graphical view ]
    Pfami PF03483. B3_4. 1 hit.
    PF03484. B5. 1 hit.
    PF03147. FDX-ACB. 1 hit.
    PF01588. tRNA_bind. 1 hit.
    [Graphical view ]
    SMARTi SM00873. B3_4. 1 hit.
    SM00874. B5. 1 hit.
    SM00896. FDX-ACB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46955. SSF46955. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF54991. SSF54991. 1 hit.
    SSF56037. SSF56037. 1 hit.
    TIGRFAMsi TIGR00472. pheT_bact. 1 hit.
    PROSITEi PS51483. B5. 1 hit.
    PS51447. FDX_ACB. 1 hit.
    PS50886. TRBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the Escherichia coli pheST operon and identification of the himA gene."
      Mechulman Y., Fayat G., Blanquet S.
      J. Bacteriol. 163:787-791(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Miller H.I.
      Submitted (NOV-1986) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.

    Entry informationi

    Entry nameiSYFB_ECOLI
    AccessioniPrimary (citable) accession number: P07395
    Secondary accession number(s): Q59407
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3