P17921 (SYFA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phenylalanine--tRNA ligase alpha chain
EC=6.1.1.20

Alternative name(s):
Phenylalanyl-tRNA synthetase alpha chain
Short name=PheRS

Gene names

Name:	pheS
Ordered Locus Names:	BSU28640

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. HAMAP MF_00281
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.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phenylalanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phenylalanine-tRNA ligase activity Inferred from electronic annotation. Source: EC tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 344	344	Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281		PRO_0000126666
Sites
	Metal binding	256	1	Magnesium By similarity
Experimental info
	Sequence conflict	90 – 105	16	GQTID…PVAVG → DRQLTSRCREPCCSR in CAA37224. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P17921 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 41C4AB7A81134C46	FASTA	344	38,675
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X53057 Genomic DNA. Translation: CAA37224.1. Z75208 Genomic DNA. Translation: CAA99603.1. AL009126 Genomic DNA. Translation: CAB14824.1.
PIR	YFBSA. H69675.
RefSeq	NP_390742.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P17921.
SMR	P17921. Positions 7-342.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000002740; EBBACP00000002740; EBBACG00000002735.
GeneID	937987.
GenomeReviews	Gene locus BSU28640 in contig AL009126_GR.
KEGG	bsu:BSU28640.
NMPDR	fig|224308.1.peg.2867.
PATRIC	18977616. VBIBacSub10457_2996.
Organism-specific databases
GenoList	BSU28640. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000002461.
HOGENOM	HBG284353.
OMA	FRASYFP.
PhylomeDB	P17921.
ProtClustDB	PRK00488.
Enzyme and pathway databases
BioCyc	BSUB:BSU28640-MONOMER.
Family and domain databases
HAMAP	MF_00281. Phe_tRNA_synth_alpha1. [Tree]
InterPro	IPR006195. aa-tRNA-synth_II. IPR004529. Phe-tRNA-synth_IIc_asu. IPR004188. Phe-tRNA_synth_II_N. IPR022911. Phe_tRNA_synth_alpha1_bac. IPR002319. Phenylalanyl-tRNA_Synthase. IPR010978. tRNA-bd_arm. [Graphical view]
KO	K01889.
Pfam	PF02912. Phe_tRNA-synt_N. 1 hit. PF01409. tRNA-synt_2d. 1 hit. [Graphical view]
SUPFAM	SSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMs	TIGR00468. PheS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYFA_BACSU

Accession

Primary (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:	January 25, 2012
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program