A7GTL0 (SYFA_BACCN) 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:	Bcer98_3249

Organism

Bacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]

Taxonomic identifier

315749 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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 By similarity 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 – 344	344	Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281		PRO_1000078825
Sites
	Metal binding	256	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7GTL0 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: A9249B9E88850449	FASTA	344	39,049
	10 20 30 40 50 60 MEARLKELKQ KALKLIEEAK ELKSLNDVRV AYLGKKGPIT EVLRGMGKLS PEERPRMGAL 70 80 90 100 110 120 VNEVREAIQT RLEEKVSNLE KAVMEAKLAS ETIDVTLPGR PVETGCHHPL TAVVEQIEDV 130 140 150 160 170 180 FIGMGYEVAE GTEVEKDYYN FEALNLPKDH PARDMQDTFY ITEETLLRTH TSSVQARTME 190 200 210 220 230 240 NNKEKGPIKI ICPGKVYRRD DDDATHSHQF MQIEGLVIDK NIRMSDLKGT LQVFVKKMFG 250 260 270 280 290 300 EDREIRLRPS FFPFTEPSVE MDISCMMCHG KGCGTCKGTG WIEILGAGMV HPNVLEMAGY 310 320 330 340 DSKEYQGFAF GMGAERIAML KYGVDDIRHF YTNDVRFLQQ FKRA

References

[1]

"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity." Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A. Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NVH 391-98.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000764 Genomic DNA. Translation: ABS23468.1.
RefSeq	YP_001376463.1. NC_009674.1.
3D structure databases
ProteinModelPortal	A7GTL0.
SMR	A7GTL0. Positions 84-342.
ModBase	Search...
Protein-protein interaction databases
STRING	A7GTL0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000036546; EBBACP00000035597; EBBACG00000036537.
GeneID	5347086.
GenomeReviews	Gene locus Bcer98_3249 in contig CP000764_GR.
KEGG	bcy:Bcer98_3249.
PATRIC	18935140. VBIBacCyt128034_3411.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0016.
GeneTree	EBGT00050000002461.
HOGENOM	HBG284353.
OMA	FRASYFP.
ProtClustDB	PRK00488.
Enzyme and pathway databases
BioCyc	BCER315749:BCER98_3249-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_BACCN

Accession

Primary (citable) accession number: A7GTL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	September 11, 2007
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program