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Protein

Phenylalanine--tRNA ligase beta subunit

Gene

pheT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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

Mg2+By similarityNote: 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

GO - Biological processi

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.
SABIO-RKP07395.

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10710. pheT.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • phenylalanine-tRNA ligase complex Source: GO_Central
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.

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiMKFSEQW.
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:
EMBLi
GenBanki
DDBJi
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.
WP_000672380.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC74783; AAC74783; b1713.
BAA15481; BAA15481; BAA15481.
GeneIDi945382.
KEGGieco:b1713.
PATRICi32118732. VBIEscCol129921_1784.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000672380.1. NZ_CP010445.1.

3D structure databases

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

Protein-protein interaction databases

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

2D gel databases

SWISS-2DPAGEP07395.

Proteomic databases

PaxDbiP07395.
PRIDEiP07395.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74783; AAC74783; b1713.
BAA15481; BAA15481; BAA15481.
GeneIDi945382.
KEGGieco:b1713.
PATRICi32118732. VBIEscCol129921_1784.

Organism-specific databases

EchoBASEiEB0704.
EcoGeneiEG10710. pheT.

Phylogenomic databases

eggNOGiCOG0073.
HOGENOMiHOG000292085.
InParanoidiP07395.
KOiK01890.
OMAiMKFSEQW.
OrthoDBiEOG6CCH1J.
PhylomeDBiP07395.

Enzyme and pathway databases

BioCyciEcoCyc:PHET-MONOMER.
ECOL316407:JW1703-MONOMER.
MetaCyc:PHET-MONOMER.
SABIO-RKP07395.

Miscellaneous databases

PROiP07395.

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]
ProtoNetiSearch...

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: July 22, 2015
This is version 145 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.