RegulonDB

Gene
Name:	lysU
Synonym(s):	ECK4123, EG10553, b4129
Genome position(nucleotides):	4353200 <-- 4354717
Strand:	reverse
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	47.43
External database links:

ASAP:	ABE-0013520
CGSC:	16693
ECHOBASE:	EB0548
ECOLIHUB:	lysU
MIM:	613641
MIM:	613916
OU-MICROARRAY:	b4129
STRING:	511145.b4129
COLOMBOS:	lysU

Gene

Name:

lysU

Synonym(s):

ECK4123, EG10553, b4129

Genome position(nucleotides):

4353200 <-- 4354717

Strand:

reverse

Sequence:

Get nucleotide sequence FastaFormat

GC content %:

47.43

External database links:

ASAP:

CGSC:

ECHOBASE:

ECOLIHUB:

MIM:

MIM:

OU-MICROARRAY:

STRING:

COLOMBOS:

Shine dalgarno
Sequence:	agctggatttAGAGGAaccaaAAT

Shine dalgarno

Sequence:

agctggatttAGAGGAaccaaAAT

Product

Name:

lysine—tRNA ligase/Ap₄A synthetase/Ap₃A synthetase

Synonym(s):

LysU

Sequence:

Get amino acid sequence Fasta Format

Cellular location:

cytosol,membrane

Molecular weight:

57.827

Isoelectric point:

4.863

Motif(s):

Type	Positions	Sequence	Comment
	2 -> 505	SEQETRGANEAIDFNDELRNRREKLAALRQQGVAFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQK	UniProt: Lysine--tRNA ligase, heat inducible.
	68 -> 146	VSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLL
	125 -> 125	R	UniProt: In Ref. 3; AAA24096..
	162 -> 501	DQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAM
	236 -> 236	L	UniProt: In Ref. 3; AAA24096..

Classification:

Multifun Terms (GenProtEC)
Multifun Terms (GenProtEC)		2 - information transfer --> 2.3 - protein related --> 2.3.1 - amino acid -activation
Gene Ontology Terms (GO)
	cellular_component	GO:0005737 - cytoplasm GO:0005829 - cytosol GO:0016020 - membrane
	molecular_function	GO:0003676 - nucleic acid binding GO:0046872 - metal ion binding GO:0016874 - ligase activity GO:0004812 - aminoacyl-tRNA ligase activity GO:0004824 - lysine-tRNA ligase activity GO:0000049 - tRNA binding GO:0000166 - nucleotide binding GO:0005524 - ATP binding GO:0000287 - magnesium ion binding GO:0042803 - protein homodimerization activity
	biological_process	GO:0006412 - translation GO:0006418 - tRNA aminoacylation for protein translation GO:0006430 - lysyl-tRNA aminoacylation GO:0034605 - cellular response to heat GO:0036260 - RNA capping

Note(s):

Note(s): ...[more].

Reference(s):

[1] Boonyalai N., et al., 2013
[2] Boy E., et al., 1976
[3] Coste H., et al., 1987
[4] Dittgen RM., et al., 1976
[5] Hirshfield IN., et al., 1977
[6] Hirshfield IN., et al., 1984
[7] Hirshfield IN., et al., 1972
[8] Hirshfield IN., et al., 1976
[9] Hirshfield IN., et al., 1975
[10] Hirshfield IN., et al., 1976
[11] Hirshfield IN., et al., 1972
[12] Hughes RA., et al., 2010
[13] Kim JJ., et al., 1981
[14] Lagerkvist U., et al., 1977
[15] Matthews RG., et al., 1988
[16] Neidhardt FC., et al., 1977
[17] Onesti S., et al., 1994
[18] Plateau P., et al., 1982
[19] Plateau P., et al., 1981
[20] Prabhu NS., et al., 2017
[21] Randerath K., et al., 1966
[22] Rapaport E., et al., 1975
[23] Reinisch F., et al., 1975
[24] Saluta MV., et al., 1995
[25] Stern R., et al., 1965
[26] Wright M., et al., 2014
[27] Wright M., et al., 2006

External database links:

ALPHAFOLD:

DIP:

ECOCYC:

ECOLIWIKI:

INTERPRO:

INTERPRO:

INTERPRO:

INTERPRO:

INTERPRO:

INTERPRO:

INTERPRO:

INTERPRO:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PFAM:

PFAM:

PRIDE:

PRINTS:

PRODB:

PROSITE:

REFSEQ:

SMR:

UNIPROT:

Transcriptional Regulation
	Display Regulation
Repressed by:	Lrp

Transcriptional Regulation

Display Regulation

Repressed by:

Lrp

RNA cis-regulatory element

Attenuation:	Translational

RNA cis-regulatory element

Attenuation:

Translational

Reference(s)
[1] Boonyalai N., Pullen JR., Abdul Wahab MF., Wright M., Miller AD., 2013, Escherichia coli LysU is a potential surrogate for human lysyl tRNA synthetase in interactions with the C-terminal domain of HIV-1 capsid protein., Org Biomol Chem 11(4):612-20
[2] Boy E., Reinisch F., Richaud C., Patte JC., 1976, Role of lysyl-tRNA in the regulation of lysine biosynthesis in Escherichia coli K12., Biochimie 58(1-2):213-8
[3] Coste H., Brevet A., Plateau P., Blanquet S., 1987, Non-adenylylated bis(5'-nucleosidyl) tetraphosphates occur in Saccharomyces cerevisiae and in Escherichia coli and accumulate upon temperature shift or exposure to cadmium., J Biol Chem 262(25):12096-103
[4] Dittgen RM., Leberman R., 1976, Multiple forms of lysyl-tRNA synthetase from Escherichia coli., Hoppe Seylers Z Physiol Chem 357(4):543-51
[5] Hirshfield IN., Liu C., Yeh FM., 1977, Two modes of metabolic regulation of lysyl-transfer ribonucleic acid synthetase in Escherichia coli K-12., J Bacteriol 131(2):589-97
[6] Hirshfield IN., Tenreiro R., Vanbogelen RA., Neidhardt FC., 1984, Escherichia coli K-12 lysyl-tRNA synthetase mutant with a novel reversion pattern., J Bacteriol 158(2):615-20
[7] Hirshfield IN., Tomford JW., Zamecnik PC., 1972, Thiosine-resistant mutants of Escherichia coli K-12 with growth-medium-dependent lysyl-tRNA synthetase activity.II. Evidence for an altered lysyl-tRNA synthetase., Biochim Biophys Acta 259(3):344-56
[8] Hirshfield IN., Yeh FM., 1976, An in vivo effect of the metabolites L-alanine and glycyl-L-leucine on the properties of the lysyl-tRNA synthetase from Escherichia coli K-12. II. Kinetic evidence., Biochim Biophys Acta 435(3):306-14
[9] Hirshfield IN., Yeh FM., Sawyer LE., 1975, Metabolites influence control of lysine transfer ribonucleic acid synthetase formation in Escherichia coli K-12., Proc Natl Acad Sci U S A 72(4):1364-7
[10] Hirshfield IN., Yeh FM., Zamecnik PC., 1976, An in vivo effect of the metabolites L-alanine and glycyl-L-leucine on the properties of lysyl-tRNA synthetase from Escherichia coli K-12. I. Influence on subunit composition and molecular weight distribution., Biochim Biophys Acta 435(3):290-305
[11] Hirshfield IN., Zamecnik PC., 1972, Thiosine-resistant mutants of Escherichia coli K-12 with growth-medium-dependent lysl-tRNA synthetase activity. I. Isolation and physiological characterization., Biochim Biophys Acta 259(3):330-43
[12] Hughes RA., Ellington AD., 2010, Rational design of an orthogonal tryptophanyl nonsense suppressor tRNA., Nucleic Acids Res 38(19):6813-30
[13] Kim JJ., Mehler AH., 1981, Stimulation of the transfer reaction of aminoacyl-tRNA synthetases by cations., Arch Biochem Biophys 209(2):465-70
[14] Lagerkvist U., Akesson B., Branden R., 1977, Aminoacyl adenylate, a normal intermediate or a dead end in aminoacylation of transfer ribonucleic acid., J Biol Chem 252(3):1002-6
[15] Matthews RG., Neidhardt FC., 1988, Abnormal induction of heat shock proteins in an Escherichia coli mutant deficient in adenosylmethionine synthetase activity., J Bacteriol 170(4):1582-8
[16] Neidhardt FC., Bloch PL., Pedersen S., Reeh S., 1977, Chemical measurement of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in Escherichia coli., J Bacteriol 129(1):378-87
[17] Onesti S., Theoclitou ME., Pernilla E., Wittung L., Miller AD., Plateau P., Blanquet S., Brick P., 1994, Crystallization and preliminary diffraction studies of Escherichia coli lysyl-tRNA synthetase (LysU)., J Mol Biol 243(1):123-5
[18] Plateau P., Blanquet S., 1982, Zinc-dependent synthesis of various dinucleoside 5',5' ' '-P1,P3-Tri- or 5'',5' ' '-P1,P4-tetraphosphates by Escherichia coli lysyl-tRNA synthetase., Biochemistry 21(21):5273-9
[19] Plateau P., Gueron M., Blanquet S., 1981, Determination of dinucleoside 5', 5"'-P1, P4- tetraphosphates by 31P and 1H NMR spectroscopy., Biochimie 63(11-12):827-30
[20] Prabhu NS., Yun H., 2017, Comparative analysis of polyspecificity of the endogenous tRNA synthetase of different expression host towards photocrosslinking amino acids using an in silico approach., J Mol Graph Model 75:375-382
[21] Randerath K., Janeway CM., Stephenson ML., Zamecnik PC., 1966, Isolation and characterization of dinucleoside tetra- and tri-phosphates formed in the presence of lysyl-sRNA synthetase., Biochem Biophys Res Commun 24(1):98-105
[22] Rapaport E., Svihovec SK., Zamecnik PC., 1975, Relationship of the first step in protein synthesis to ppGpp: formation of A(5')ppp(5')Gpp., Proc Natl Acad Sci U S A 72(7):2653-7
[23] Reinisch F., Boy E., Patte JC., 1975, [Regulation of lysyl-tRNA synthetase of Escherichia coli K12]., C R Acad Sci Hebd Seances Acad Sci D 280(17):2041-3
[24] Saluta MV., Hirshfield IN., 1995, The occurrence of duplicate lysyl-tRNA synthetase gene homologs in Escherichia coli and other procaryotes., J Bacteriol 177(7):1872-8
[25] Stern R., Mehler AH., 1965, Lysyl-sRNA synthetase from Escherichia coli., Biochem Z 342(4):400-9
[26] Wright M., Azhar MA., Kamal A., Miller AD., 2014, Syntheses of stable, synthetic diadenosine polyphosphate analogues using recombinant histidine-tagged lysyl tRNA synthetase (LysU)., Bioorg Med Chem Lett 24(10):2346-52
[27] Wright M., Miller AD., 2006, Novel fluorescent labelled affinity probes for diadenosine-5',5'''-P1,P4-tetraphosphate (Ap4A)-binding studies., Bioorg Med Chem Lett 16(4):943-8

Reference(s)

[1] Boonyalai N., Pullen JR., Abdul Wahab MF., Wright M., Miller AD., 2013, Escherichia coli LysU is a potential surrogate for human lysyl tRNA synthetase in interactions with the C-terminal domain of HIV-1 capsid protein., Org Biomol Chem 11(4):612-20