Reviewed, UniProtKB/Swiss-Prot P07395 (SYFB_ECOLI)

Names and origin

Protein names

Recommended name:
    Phenylalanyl-tRNA synthetase beta chain
    EC=6.1.1.20
Alternative name(s):
    Phenylalanine--tRNA ligase beta chain
      Short name=PheRS

Gene names

Name:	pheT
Ordered Locus Names:	b1713, JW1703

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	795 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP MF_00283
Cofactor	Binds 2 magnesium ions per tetramer By similarity.
Subunit structure	Tetramer of two alpha and two beta chains. HAMAP MF_00283
Subcellular location	Cytoplasm. HAMAP MF_00283
Sequence similarities	Belongs to the phenylalanyl-tRNA synthetase beta chain family. Type 1 subfamily. Contains 1 FDX-ACB domain. Contains 1 tRNA-binding domain.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding RNA-binding tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phenylalanyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP tRNA processing Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB membrane Inferred from direct assay. Source: UniProtKB
Molecular function	ATP 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 protein binding Inferred from physical interaction. Source: IntAct tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
pheS	P08312	1	EBI-555713,EBI-555676
rpsB	P0A7V0	1	EBI-555713,EBI-543439

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 795	795	Phenylalanyl-tRNA synthetase beta chain HAMAP MF_00283		PRO_0000126880
Regions
	Domain	39 – 148	110	tRNA-binding
	Domain	701 – 794	94	FDX-ACB
Sites
	Metal binding	454	1	Magnesium By similarity
	Metal binding	460	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	463	1	Magnesium By similarity
	Metal binding	464	1	Magnesium By similarity
Experimental info
	Sequence conflict	93	1	A → T in CAA23565. Ref.1
	Sequence conflict	141 – 142	2	AP → VR in CAA23565. Ref.1
	Sequence conflict	186 – 189	4	PLVQ → AAGN in CAA23565. Ref.1
	Sequence conflict	481	1	A → R in CAA23565. Ref.1
	Sequence conflict	698	1	R → G in CAA23565. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P07395-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 3B55EC65D25937E5	FASTA	795	87,378
	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

References

	« Hide 'large scale' referencesShow '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: 2991205] [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. , 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: 9097039] [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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBLGenBankDDBJ	V00291 Genomic DNA. Translation: CAA23565.1. K02844 Genomic DNA. Translation: AAA51470.1. U00096 Genomic DNA. Translation: AAC74783.1. AP009048 Genomic DNA. Translation: BAA15481.1.
PIR	SYECFB. I41284.
RefSeq	AP_002333.1. NP_416228.1.
3D structure databases
HSSP	HSSP built from PDB template 1JJC based on UniProtKB P27002.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6879N.
IntAct	P07395. 12 interactions.
2-D gel databases
SWISS-2DPAGE	P07395.
ECO2DBASE	D094.0. 6TH EDITION.
Genome annotation databases
GeneID	945382.
GenomeReviews	Gene locus JW1703 in contig AP009048_GR. Gene locus b1713 in contig U00096_GR.
KEGG	ecj:JW1703. eco:b1713.
Organism-specific databases
EchoBASE	EB0704.
EcoGene	EG10710. pheT.
CMR	Search...
Phylogenomic databases
HOGENOM	P07395.
OMA	P07395. MHAFDLA.
Enzyme and pathway databases
BioCyc	EcoCyc:PHET-MON. MetaCyc:PHET-MON.
Family and domain databases
HAMAP	MF_00283. [Tree]
InterPro	IPR005146. B3/B4_tRNA-bd. IPR005147. B5. IPR012340. NA-bd_OB-fold. IPR004532. Phe-tRNA-synth_IIc_bsu_bac. IPR005121. PheS_beta_Fdx_antiC_bd. IPR002547. tRNA_bd. [Graphical view]
Gene3D	G3DSA:3.50.40.10. B3_4. 1 hit. G3DSA:3.30.56.20. B5. 1 hit. G3DSA:3.30.70.380. Fdx_AntiC_bd. 1 hit. G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
Pfam	PF03483. B3_4. 1 hit. PF03484. B5. 1 hit. PF03147. FDX-ACB. 1 hit. PF01588. tRNA_bind. 1 hit. [Graphical view]
TIGRFAMs	TIGR00472. pheT_bact. 1 hit.
PROSITE	PS51447. FDX_ACB. 1 hit. PS50886. TRBD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYFB_ECOLI

Accession

Primary (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:	June 16, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)