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Protein

Phenylalanine--tRNA ligase beta subunit

Gene

pheT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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)DescriptionActionsGraphical viewLength
Metal bindingi454MagnesiumBy similarity1
Metal bindingi460Magnesium; via carbonyl oxygenBy similarity1
Metal bindingi463MagnesiumBy similarity1
Metal bindingi464MagnesiumBy similarity1

GO - Molecular functioni

GO - Biological processi

  • phenylalanyl-tRNA aminoacylation Source: EcoCyc
  • 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.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10710. pheT.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • membrane Source: UniProtKB
  • phenylalanine-tRNA ligase complex Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001268801 – 795Phenylalanine--tRNA ligase beta subunitAdd BLAST795

Proteomic databases

EPDiP07395.
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

BioGridi4262088. 189 interactors.
DIPiDIP-6879N.
IntActiP07395. 12 interactors.
MINTiMINT-1231494.
STRINGi511145.b1713.

Structurei

Secondary structure

1795
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 4Combined sources3
Helixi5 – 9Combined sources5
Helixi20 – 26Combined sources7
Turni27 – 29Combined sources3
Beta strandi31 – 39Combined sources9
Beta strandi45 – 54Combined sources10
Beta strandi64 – 68Combined sources5
Beta strandi70 – 73Combined sources4
Beta strandi75 – 78Combined sources4
Beta strandi89 – 93Combined sources5
Beta strandi108 – 119Combined sources12
Helixi123 – 125Combined sources3
Helixi147 – 150Combined sources4
Beta strandi156 – 161Combined sources6
Helixi172 – 183Combined sources12
Turni210 – 212Combined sources3
Beta strandi214 – 223Combined sources10
Helixi233 – 240Combined sources8
Helixi249 – 260Combined sources12
Beta strandi264 – 268Combined sources5
Helixi269 – 271Combined sources3
Beta strandi277 – 279Combined sources3
Beta strandi287 – 289Combined sources3
Turni290 – 292Combined sources3
Beta strandi293 – 295Combined sources3
Beta strandi303 – 305Combined sources3
Beta strandi307 – 313Combined sources7
Turni314 – 316Combined sources3
Beta strandi331 – 337Combined sources7
Helixi340 – 342Combined sources3
Helixi346 – 349Combined sources4
Helixi355 – 362Combined sources8
Helixi369 – 381Combined sources13
Beta strandi387 – 395Combined sources9
Turni397 – 399Combined sources3
Beta strandi405 – 409Combined sources5
Helixi410 – 417Combined sources8
Helixi423 – 433Combined sources11
Beta strandi436 – 440Combined sources5
Beta strandi443 – 447Combined sources5
Helixi458 – 469Combined sources12
Helixi471 – 473Combined sources3
Beta strandi480 – 482Combined sources3
Helixi495 – 504Combined sources10
Beta strandi514 – 516Combined sources3
Helixi518 – 524Combined sources7
Beta strandi525 – 527Combined sources3
Beta strandi546 – 548Combined sources3
Helixi549 – 560Combined sources12
Beta strandi568 – 578Combined sources11
Beta strandi586 – 601Combined sources16
Beta strandi605 – 607Combined sources3
Helixi614 – 624Combined sources11
Turni625 – 627Combined sources3
Beta strandi644 – 652Combined sources9
Turni654 – 656Combined sources3
Beta strandi660 – 665Combined sources6
Turni667 – 673Combined sources7
Beta strandi679 – 685Combined sources7
Helixi686 – 688Combined sources3
Beta strandi689 – 691Combined sources3
Beta strandi706 – 715Combined sources10
Helixi720 – 724Combined sources5
Turni725 – 727Combined sources3
Turni730 – 734Combined sources5
Beta strandi735 – 740Combined sources6
Beta strandi753 – 762Combined sources10
Helixi771 – 784Combined sources14
Turni785 – 789Combined sources5

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 148tRNA-bindingAdd BLAST110
Domaini401 – 476B5Add BLAST76
Domaini701 – 794FDX-ACBAdd BLAST94

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C6A. Bacteria.
COG0072. LUCA.
COG0073. LUCA.
HOGENOMiHOG000292085.
InParanoidiP07395.
KOiK01890.
OMAiMKFSEQW.
PhylomeDBiP07395.

Family and domain databases

CDDicd02796. tRNA_bind_bactPheRS. 1 hit.
Gene3Di3.30.56.20. 1 hit.
3.30.70.380. 1 hit.
3.50.40.10. 1 hit.
HAMAPiMF_00283. Phe_tRNA_synth_beta1. 1 hit.
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.
IPR033714. tRNA_bind_bactPheRS.
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)DescriptionActionsGraphical viewLength
Sequence conflicti93A → T in CAA23565 (PubMed:2991205).Curated1
Sequence conflicti141 – 142AP → VR in CAA23565 (PubMed:2991205).Curated2
Sequence conflicti186 – 189PLVQ → AAGN in CAA23565 (PubMed:2991205).Curated4
Sequence conflicti481A → R in CAA23565 (PubMed:2991205).Curated1
Sequence conflicti698R → G in CAA23565 (PubMed:2991205).Curated1

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_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74783; AAC74783; b1713.
BAA15481; BAA15481; BAA15481.
GeneIDi945382.
KEGGiecj:JW1703.
eco: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_LN832404.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi4262088. 189 interactors.
DIPiDIP-6879N.
IntActiP07395. 12 interactors.
MINTiMINT-1231494.
STRINGi511145.b1713.

2D gel databases

SWISS-2DPAGEP07395.

Proteomic databases

EPDiP07395.
PaxDbiP07395.
PRIDEiP07395.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74783; AAC74783; b1713.
BAA15481; BAA15481; BAA15481.
GeneIDi945382.
KEGGiecj:JW1703.
eco:b1713.
PATRICi32118732. VBIEscCol129921_1784.

Organism-specific databases

EchoBASEiEB0704.
EcoGeneiEG10710. pheT.

Phylogenomic databases

eggNOGiENOG4105C6A. Bacteria.
COG0072. LUCA.
COG0073. LUCA.
HOGENOMiHOG000292085.
InParanoidiP07395.
KOiK01890.
OMAiMKFSEQW.
PhylomeDBiP07395.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP07395.

Family and domain databases

CDDicd02796. tRNA_bind_bactPheRS. 1 hit.
Gene3Di3.30.56.20. 1 hit.
3.30.70.380. 1 hit.
3.50.40.10. 1 hit.
HAMAPiMF_00283. Phe_tRNA_synth_beta1. 1 hit.
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.
IPR033714. tRNA_bind_bactPheRS.
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...

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: November 2, 2016
This is version 154 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

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 one 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.