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Reviewed, UniProtKB/Swiss-Prot P17921 (SYFA_BACSU)

Last modified November 3, 2009. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Phenylalanyl-tRNA synthetase alpha chain
    EC=6.1.1.20
Alternative name(s):
    Phenylalanine--tRNA ligase alpha chain
      Short name=PheRS
Gene names
Name: pheS
Ordered Locus Names: BSU28640
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP MF_00281

Cofactor

Binds 2 magnesium ions per tetramer By similarity.

Subunit structure

Tetramer of two alpha and two beta chains By similarity.

Subcellular location

Cytoplasm. HAMAP MF_00281

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha chain type 1 subfamily.

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphenylalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: HAMAP

phenylalanine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Phenylalanyl-tRNA synthetase alpha chain HAMAP MF_00281
PRO_0000126666

Sites

Metal binding2561Magnesium By similarity

Experimental info

Sequence conflict90 – 10516GQTID…PVAVG → DRQLTSRCREPCCSR in CAA37224. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P17921-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 41C4AB7A81134C46

FASTA34438,675
        10         20         30         40         50         60 
MEEKLKQLEQ EALEQVEAAS SLKVVNDIRV QYLGKKGPIT EVLRGMGKLS AEERPKMGAL 

        70         80         90        100        110        120 
ANEVRERIAN AIADKNEKLE EEEMKQKLAG QTIDVTLPGN PVAVGGRHPL TVVIEEIEDL 

       130        140        150        160        170        180 
FIGMGYTVEE GPEVETDYYN FESLNLPKEH PARDMQDSFY ITEETLMRTQ TSPVQTRTME 

       190        200        210        220        230        240 
KHEGKGPVKI ICPGKVYRRD NDDATHSHQF MQIEGLVVDK NISMSDLKGT LELVAKKMFG 

       250        260        270        280        290        300 
QDREIRLRPS FFPFTEPSVE VDVTCFKCGG NGCSVCKGTG WIEILGAGMV HPNVLKMAGF 

       310        320        330        340 
DPKEYQGFAF GMGVERIAML KYGIDDIRHF YTNDVRFISQ FKQA

« Hide

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References

« Hide 'large scale' references
[1]"Structure and nucleotide sequence of the Bacillus subtilis phenylalanyl-tRNA synthetase genes."
Brakhage A., Wozny M., Putzer H.
Biochimie 72:725-734(1990) [PubMed: 2127701] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]Erratum
Brakhage A., Wozny M., Putzer H.
Biochimie 73:127-127(1991) [PubMed: 1903307] [Abstract]
[3]"The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism."
Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R.
Microbiology 142:3067-3078(1996) [PubMed: 8969504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

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Cross-references

Sequence databases

X53057 Genomic DNA. Translation: CAA37224.1.
Z75208 Genomic DNA. Translation: CAA99603.1.
AL009126 Genomic DNA. Translation: CAB14824.1.
PIRYFBSA. H69675.
RefSeqNP_390742.1.

3D structure databases

HSSPHSSP built from PDB template 1JJC based on UniProtKB P27001.
ModBaseSearch...

Genome annotation databases

GeneID937987.
GenomeReviewsGene locus BSU28640 in contig AL009126_GR.
KEGGbsu:BSU28640.
NMPDRfig|224308.1.peg.2867.

Organism-specific databases

SubtiListBG10874. pheS. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP17921.
OMAFRASYFP.

Enzyme and pathway databases

BioCycBSUB224308:BSU2860-MON.
BRENDA6.1.1.20. 150.

Family and domain databases

HAMAPMF_00281.
[Tree]
InterProIPR006195. aa-tRNA-synth_II_cons-reg.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR004188. Phe-tRNA_synth_II_N.
IPR002319. Phenylalanyl-tRNA_Synthase_acu.
[Graphical view]
PANTHERPTHR11538. tRNA-synt_2d. 1 hit.
PfamPF02912. Phe_tRNA-synt_N. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
TIGRFAMsTIGR00468. pheS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSYFA_BACSU
AccessionPrimary (citable) accession number: P17921
Secondary accession number(s): P94539
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1997
Last modified: November 3, 2009
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents