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P07395 (SYFB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phenylalanine--tRNA ligase beta subunit
EC=6.1.1.20
Alternative name(s):
Phenylalanyl-tRNA synthetase beta subunit
Short name=PheRS
Gene names
Name:pheT
Ordered Locus Names:b1713, JW1703
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length795 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP-Rule MF_00283

Cofactor

Binds 2 magnesium ions per tetramer By similarity.

Subunit structure

Tetramer of two alpha and two beta subunits.

Subcellular location

Cytoplasm HAMAP-Rule MF_00283.

Sequence similarities

Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.

Contains 1 B5 domain.

Contains 1 FDX-ACB domain.

Contains 1 tRNA-binding domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

pheSP083125EBI-555713,EBI-555676

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 795795Phenylalanine--tRNA ligase beta subunit HAMAP-Rule MF_00283
PRO_0000126880

Regions

Domain39 – 148110tRNA-binding
Domain401 – 47676B5
Domain701 – 79494FDX-ACB

Sites

Metal binding4541Magnesium By similarity
Metal binding4601Magnesium; via carbonyl oxygen By similarity
Metal binding4631Magnesium By similarity
Metal binding4641Magnesium By similarity

Experimental info

Sequence conflict931A → T in CAA23565. Ref.1
Sequence conflict141 – 1422AP → VR in CAA23565. Ref.1
Sequence conflict186 – 1894PLVQ → AAGN in CAA23565. Ref.1
Sequence conflict4811A → R in CAA23565. Ref.1
Sequence conflict6981R → G in CAA23565. Ref.1

Secondary structure

1 ............................................................................................................................ 795
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07395 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 3B55EC65D25937E5

FASTA79587,378
        10         20         30         40         50         60 
MKFSELWLRE WVNPAIDSDA LANQITMAGL EVDGVEPVAG SFHGVVVGEV VECAQHPNAD 

        70         80         90        100        110        120 
KLRVTKVNVG GDRLLDIVCG APNCRQGLRV AVATIGAVLP GDFKIKAAKL RGEPSEGMLC 

       130        140        150        160        170        180 
SFSELGISDD HSGIIELPAD APIGTDIREY LKLDDNTIEI SVTPNRADCL GIIGVARDVA 

       190        200        210        220        230        240 
VLNQLPLVQP EIVPVGATID DTLPITVEAP EACPRYLGRV VKGINVKAPT PLWMKEKLRR 

       250        260        270        280        290        300 
CGIRSIDAVV DVTNYVLLEL GQPMHAFDKD RIEGGIVVRM AKEGETLVLL DGTEAKLNAD 

       310        320        330        340        350        360 
TLVIADHNKA LAMGGIFGGE HSGVNDETQN VLLECAFFSP LSITGRARRH GLHTDASHRY 

       370        380        390        400        410        420 
ERGVDPALQH KAMERATRLL IDICGGEAGP VIDITNEATL PKRATITLRR SKLDRLIGHH 

       430        440        450        460        470        480 
IADEQVTDIL RRLGCEVTEG KDEWQAVAPS WRFDMEIEED LVEEVARVYG YNNIPDEPVQ 

       490        500        510        520        530        540 
ASLIMGTHRE ADLSLKRVKT LLNDKGYQEV ITYSFVDPKV QQMIHPGVEA LLLPSPISVE 

       550        560        570        580        590        600 
MSAMRLSLWT GLLATVVYNQ NRQQNRVRIF ESGLRFVPDT QAPLGIRQDL MLAGVICGNR 

       610        620        630        640        650        660 
YEEHWNLAKE TVDFYDLKGD LESVLDLTGK LNEVEFRAEA NPALHPGQSA AIYLKGERIG 

       670        680        690        700        710        720 
FVGVVHPELE RKLDLNGRTL VFELEWNKLA DRVVPQAREI SRFPANRRDI AVVVAENVPA 

       730        740        750        760        770        780 
ADILSECKKV GVNQVVGVNL FDVYRGKGVA EGYKSLAISL ILQDTSRTLE EEEIAATVAK 

       790 
CVEALKERFQ ASLRD

« Hide

References

« Hide 'large scale' references
[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]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		V00291 Genomic DNA. Translation: CAA23565.1.
K02844 Genomic DNA. Translation: AAA51470.1.
U00096 Genomic DNA. Translation: AAC74783.1.
AP009048 Genomic DNA. Translation: BAA15481.1.
PIRSYECFB. I41284.
RefSeqNP_416228.1. NC_000913.2.
YP_489975.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PCOX-ray3.02B/D1-795[»]
ProteinModelPortalP07395.
SMRP07395. Positions 1-795.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6879N.
IntActP07395. 12 interactions.
MINTMINT-1231494.
STRING511145.b1713.

2D gel databases

SWISS-2DPAGEP07395.

Proteomic databases

PaxDbP07395.
PRIDEP07395.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74783; AAC74783; b1713.
BAA15481; BAA15481; BAA15481.
GeneID12933094.
945382.
KEGGecj:Y75_p1688.
eco:b1713.
PATRIC32118732. VBIEscCol129921_1784.

Organism-specific databases

EchoBASEEB0704.
EcoGeneEG10710. pheT.

Phylogenomic databases

eggNOGCOG0073.
HOGENOMHOG000292085.
KOK01890.
OMAMKFSEQW.
ProtClustDBPRK00629.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP07395.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.30.56.20. 1 hit.
3.30.70.380. 1 hit.
3.50.40.10. 1 hit.
HAMAPMF_00283. Phe_tRNA_synth_beta1.
InterProIPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR012340. NA-bd_OB-fold.
IPR004532. Phe-tRNA-ligase_IIc_bsu_bac.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR005121. PheS_beta_Fdx_antiC-bd.
IPR002547. tRNA-bd_dom.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view]
PfamPF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
PF03147. FDX-ACB. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
SMARTSM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
SM00896. FDX-ACB. 1 hit.
[Graphical view]
SUPFAMSSF56037. B3_4. 1 hit.
SSF54991. Fdx_AntiC_bd. 1 hit.
SSF50249. Nucleic_acid_OB. 1 hit.
SSF46955. Putativ_DNA_bind. 1 hit.
TIGRFAMsTIGR00472. pheT_bact. 1 hit.
PROSITEPS51483. B5. 1 hit.
PS51447. FDX_ACB. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYFB_ECOLI
AccessionPrimary (citable) accession number: P07395
Secondary accession number(s): Q59407
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents