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P07395

- SYFB_ECOLI

UniProt

P07395 - SYFB_ECOLI

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Protein

Phenylalanine--tRNA ligase beta subunit

Gene

pheT

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

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

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-HAMAP
  2. membrane Source: UniProtKB
Complete GO annotation...

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.
InParanoidiP07395.
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

        10         20         30         40         50
MKFSELWLRE WVNPAIDSDA LANQITMAGL EVDGVEPVAG SFHGVVVGEV
60 70 80 90 100
VECAQHPNAD KLRVTKVNVG GDRLLDIVCG APNCRQGLRV AVATIGAVLP
110 120 130 140 150
GDFKIKAAKL RGEPSEGMLC SFSELGISDD HSGIIELPAD APIGTDIREY
160 170 180 190 200
LKLDDNTIEI SVTPNRADCL GIIGVARDVA VLNQLPLVQP EIVPVGATID
210 220 230 240 250
DTLPITVEAP EACPRYLGRV VKGINVKAPT PLWMKEKLRR CGIRSIDAVV
260 270 280 290 300
DVTNYVLLEL GQPMHAFDKD RIEGGIVVRM AKEGETLVLL DGTEAKLNAD
310 320 330 340 350
TLVIADHNKA LAMGGIFGGE HSGVNDETQN VLLECAFFSP LSITGRARRH
360 370 380 390 400
GLHTDASHRY ERGVDPALQH KAMERATRLL IDICGGEAGP VIDITNEATL
410 420 430 440 450
PKRATITLRR SKLDRLIGHH IADEQVTDIL RRLGCEVTEG KDEWQAVAPS
460 470 480 490 500
WRFDMEIEED LVEEVARVYG YNNIPDEPVQ ASLIMGTHRE ADLSLKRVKT
510 520 530 540 550
LLNDKGYQEV ITYSFVDPKV QQMIHPGVEA LLLPSPISVE MSAMRLSLWT
560 570 580 590 600
GLLATVVYNQ NRQQNRVRIF ESGLRFVPDT QAPLGIRQDL MLAGVICGNR
610 620 630 640 650
YEEHWNLAKE TVDFYDLKGD LESVLDLTGK LNEVEFRAEA NPALHPGQSA
660 670 680 690 700
AIYLKGERIG FVGVVHPELE RKLDLNGRTL VFELEWNKLA DRVVPQAREI
710 720 730 740 750
SRFPANRRDI AVVVAENVPA ADILSECKKV GVNQVVGVNL FDVYRGKGVA
760 770 780 790
EGYKSLAISL ILQDTSRTLE EEEIAATVAK CVEALKERFQ ASLRD
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.
InParanoidi P07395.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 140 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