Q7W7C7 (SYFA_BORPA) 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:	BPP2598

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	348 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
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 – 348	348	Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281		PRO_0000126671
Sites
	Metal binding	268	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7W7C7 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: F3CE856A786DB4AC	FASTA	348	39,172
	10 20 30 40 50 60 MRFEGSNSMT LLVDDLVSQA QERFAAASDA AALENAKARF LGKEGALTVL LKALGKLDPE 70 80 90 100 110 120 QKREMGARIN QAKQQIEALL NARRAALAQA ELDARLASET IDVTLPGRGK AAGGIHPVIR 130 140 150 160 170 180 TWERVEEIFR SIGFDVADGP EVENDWTNFT ALNNPLDHPA RSMQDTFYVD MHDADGLPLL 190 200 210 220 230 240 LRTHTSPMQV RYARMHKPPI KVIAPGRTYR VDSGATHSPM FHQVEGLWIA EDISFADLKG 250 260 270 280 290 300 VYTDFLRCFF ESDDLVVRFR PSFFPFTEPS AEIDMMFTSG PNRGRWLEIS GSGQVHPQVV 310 320 330 340 RNFGLDPERY IGFAFGSGLE RLTMLRYGVN DLRQFYEGDL RFLRQFNE

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640431 Genomic DNA. Translation: CAE37890.1.
RefSeq	NP_884822.2. NC_002928.3.
3D structure databases
ProteinModelPortal	Q7W7C7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1666354.
GenomeReviews	Gene locus BPP2598 in contig BX470249_GR.
KEGG	bpa:BPP2598.
NMPDR	fig|257311.1.peg.2456.
PATRIC	21149090. VBIBorPar43418_2725.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG284353.
OMA	FRASYFP.
PhylomeDB	Q7W7C7.
ProtClustDB	PRK00488.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP2598-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_BORPA

Accession

Primary (citable) accession number: Q7W7C7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program