RegulonDB

Gene
Name:	iscU
Synonym(s):	ECK2526, G7324, b2529, nifU, yfhN
Genome position(nucleotides):	2659903 <-- 2660289
Strand:	reverse
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	50.13
External database links:

ASAP:	ABE-0008321
ECHOBASE:	EB3176
ECOLIHUB:	iscU
MIM:	255125
OU-MICROARRAY:	b2529
STRING:	511145.b2529
COLOMBOS:	iscU

Gene

Name:

iscU

Synonym(s):

ECK2526, G7324, b2529, nifU, yfhN

Genome position(nucleotides):

2659903 <-- 2660289

Strand:

reverse

Sequence:

Get nucleotide sequence FastaFormat

GC content %:

50.13

External database links:

ASAP:

ECHOBASE:

ECOLIHUB:

MIM:

OU-MICROARRAY:

STRING:

COLOMBOS:

Type

Positions

Sequence

Comment

2 -> 126

AYSEKVIDHYENPRNVGSFDNNDENVGSGMVGAPACGDVMKLQIKVNDEGIIEDARFKTYGCGSAIASSSLVTEWVKGKSLDEAQAIKNTDIAEELELPPVKIHCSILAEDAIKAAIADYKSKRE

39 -> 39

UniProt: Stabilizes apo-protein in the S-state (structured)..

89 -> 89

UniProt: Stabilizes apo-protein in the D-state; Fe-S cluster assembly 3-fold slower than wild-type..

90 -> 90

UniProt: Stabilizes apo-protein in the D-state; Fe-S cluster assembly 3-fold slower than wild-type..

99 -> 103

LPPVK

Type

Positions

Sequence

Comment

2 -> 126

AYSEKVIDHYENPRNVGSFDNNDENVGSGMVGAPACGDVMKLQIKVNDEGIIEDARFKTYGCGSAIASSSLVTEWVKGKSLDEAQAIKNTDIAEELELPPVKIHCSILAEDAIKAAIADYKSKRE

39 -> 39

UniProt: Stabilizes apo-protein in the S-state (structured)..

89 -> 89

UniProt: Stabilizes apo-protein in the D-state; Fe-S cluster assembly 3-fold slower than wild-type..

90 -> 90

UniProt: Stabilizes apo-protein in the D-state; Fe-S cluster assembly 3-fold slower than wild-type..

99 -> 103

LPPVK

107 -> 107

UniProt: Stabilizes apo-protein in the S-state; biphasic Fe-S cluster assembly 7-fold slower than wild-type..

108 -> 108

I -> M: renders ISC system dependent on CyaY.

111 -> 111

UniProt: Stabilizes apo-protein in the S-state; biphasic Fe-S cluster assembly 7-fold slower than wild-type..

Multifun Terms (GenProtEC)

1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.3 - cofactors, small molecule carriers

1 - metabolism --> 1.8 - metabolism of other compounds --> 1.8.2 - sulfur metabolism

2 - information transfer --> 2.3 - protein related --> 2.3.3 - posttranslational modification

Gene Ontology Terms (GO)

cellular_component

GO:1990330 - IscS-IscU complex
GO:0005737 - cytoplasm
GO:0005829 - cytosol

molecular_function

GO:0005507 - copper ion binding
GO:0005515 - protein binding
GO:0008270 - zinc ion binding
GO:0051536 - iron-sulfur cluster binding
GO:0051539 - 4 iron, 4 sulfur cluster binding
GO:0051537 - 2 iron, 2 sulfur cluster binding
GO:0005506 - iron ion binding
GO:0008198 - ferrous iron binding
GO:0042802 - identical protein binding

biological_process

GO:0016226 - iron-sulfur cluster assembly
GO:0006879 - cellular iron ion homeostasis
GO:0019448 - L-cysteine catabolic process

Transcriptional Regulation
	Display Regulation
Repressed by:	IscR

Transcriptional Regulation

Display Regulation

Repressed by:

IscR

Type	Name	Post Left	Strand	Notes	Evidence (Confirmed, Strong, Weak)	References
promoter	iscAp7	2659953	reverse	nd	[COMP-AINF]	[12]
promoter	iscAp6	2659962	reverse	nd	[COMP-AINF]	[12]
promoter	TSS_2827	2661124	reverse	nd	[RS-EPT-CBR]	[13]

Type

Name

Post Left

Post Right

Strand

Notes

Evidence (Confirmed, Strong, Weak)

References

promoter

iscAp7

2659953

reverse

[COMP-AINF]

[12]

promoter

iscAp6

2659962

reverse

[COMP-AINF]

[12]

promoter

TSS_2827

2661124

reverse

[RS-EPT-CBR]

[13]

Evidence
[COMP-AINF] Inferred computationally without human oversight
[RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

Evidence

[COMP-AINF] Inferred computationally without human oversight

[RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

Reference(s)
[1] Bonomi F., Iametti S., Ta D., Vickery LE., 2005, Multiple turnover transfer of [2Fe2S] clusters by the iron-sulfur cluster assembly scaffold proteins IscU and IscA., J Biol Chem 280(33):29513-8
[2] Bridwell-Rabb J., Iannuzzi C., Pastore A., Barondeau DP., 2012, Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis., Biochemistry 51(12):2506-14
[3] Dai Y., Outten FW., 2012, The E. coli SufS-SufE sulfur transfer system is more resistant to oxidative stress than IscS-IscU., FEBS Lett 586(22):4016-22
[4] Ezraty B., Vergnes A., Banzhaf M., Duverger Y., Huguenot A., Brochado AR., Su SY., Espinosa L., Loiseau L., Py B., Typas A., Barras F., 2013, Fe-S cluster biosynthesis controls uptake of aminoglycosides in a ROS-less death pathway., Science 340(6140):1583-7
[5] Jaroschinsky M., Pinske C., Gary Sawers R., 2017, Differential effects of isc operon mutations on the biosynthesis and activity of key anaerobic metalloenzymes in Escherichia coli., Microbiology 163(6):878-890
[6] Kim JH., Tonelli M., Kim T., Markley JL., 2012, Three-dimensional structure and determinants of stability of the iron-sulfur cluster scaffold protein IscU from Escherichia coli., Biochemistry 51(28):5557-63
[7] Puglisi R., Boeri Erba E., Pastore A., 2020, A Guide to Native Mass Spectrometry to determine complex interactomes of molecular machines., FEBS J 287(12):2428-2439
[8] Wu G., Li L., 2012, Biochemical Characterization of Iron-Sulfur Cluster Assembly in the Scaffold IscU of Escherichia coli., Biochemistry (Mosc) 77(2):135-42
[9] Yan R., Adinolfi S., Pastore A., 2015, Ferredoxin, in conjunction with NADPH and ferredoxin-NADP reductase, transfers electrons to the IscS/IscU complex to promote iron-sulfur cluster assembly., Biochim Biophys Acta 1854(9):1113-7
[10] Yee N., Choi J., Porter AW., Carey S., Rauschenbach I., Harel A., 2014, Selenate reductase activity in Escherichia coli requires Isc iron-sulfur cluster biosynthesis genes., FEMS Microbiol Lett 361(2):138-43
[11] Zhang Q., Fang G., Chen W., Zhong X., Long Y., Qin H., Ye J., 2020, The molecular effects of ultrasound on the expression of cellular proteome., Sci Total Environ 720:137439
[12] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78
[13] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

Reference(s)

[1] Bonomi F., Iametti S., Ta D., Vickery LE., 2005, Multiple turnover transfer of [2Fe2S] clusters by the iron-sulfur cluster assembly scaffold proteins IscU and IscA., J Biol Chem 280(33):29513-8

[2] Bridwell-Rabb J., Iannuzzi C., Pastore A., Barondeau DP., 2012, Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis., Biochemistry 51(12):2506-14

[3] Dai Y., Outten FW., 2012, The E. coli SufS-SufE sulfur transfer system is more resistant to oxidative stress than IscS-IscU., FEBS Lett 586(22):4016-22

[4] Ezraty B., Vergnes A., Banzhaf M., Duverger Y., Huguenot A., Brochado AR., Su SY., Espinosa L., Loiseau L., Py B., Typas A., Barras F., 2013, Fe-S cluster biosynthesis controls uptake of aminoglycosides in a ROS-less death pathway., Science 340(6140):1583-7

[5] Jaroschinsky M., Pinske C., Gary Sawers R., 2017, Differential effects of isc operon mutations on the biosynthesis and activity of key anaerobic metalloenzymes in Escherichia coli., Microbiology 163(6):878-890

[6] Kim JH., Tonelli M., Kim T., Markley JL., 2012, Three-dimensional structure and determinants of stability of the iron-sulfur cluster scaffold protein IscU from Escherichia coli., Biochemistry 51(28):5557-63

[7] Puglisi R., Boeri Erba E., Pastore A., 2020, A Guide to Native Mass Spectrometry to determine complex interactomes of molecular machines., FEBS J 287(12):2428-2439

[8] Wu G., Li L., 2012, Biochemical Characterization of Iron-Sulfur Cluster Assembly in the Scaffold IscU of Escherichia coli., Biochemistry (Mosc) 77(2):135-42

[9] Yan R., Adinolfi S., Pastore A., 2015, Ferredoxin, in conjunction with NADPH and ferredoxin-NADP reductase, transfers electrons to the IscS/IscU complex to promote iron-sulfur cluster assembly., Biochim Biophys Acta 1854(9):1113-7

[10] Yee N., Choi J., Porter AW., Carey S., Rauschenbach I., Harel A., 2014, Selenate reductase activity in Escherichia coli requires Isc iron-sulfur cluster biosynthesis genes., FEMS Microbiol Lett 361(2):138-43

[11] Zhang Q., Fang G., Chen W., Zhong X., Long Y., Qin H., Ye J., 2020, The molecular effects of ultrasound on the expression of cellular proteome., Sci Total Environ 720:137439

[12] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

[13] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.