RegulonDB RegulonDB 11.1: Gene Form
   

iscU gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

iscS iscU iscA anti-anti-terminator anti-terminator TSS_2827 TSS_2827 iscAp6 iscAp6 iscAp7 iscAp7

Gene      
Name: iscU    Texpresso search in the literature
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


Product      
Name: scaffold protein for iron-sulfur cluster assembly
Synonym(s): IscU, NifU, YfhN
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 13.849
Isoelectric point: 4.558
Motif(s):
 
Type Positions Sequence Comment
2 -> 126 AYSEKVIDHYENPRNVGSFDNNDENVGSGMVGAPACGDVMKLQIKVNDEGIIEDARFKTYGCGSAIASSSLVTEWVKGKSLDEAQAIKNTDIAEELELPPVKIHCSILAEDAIKAAIADYKSKRE
39 -> 39 D UniProt: Stabilizes apo-protein in the S-state (structured)..
89 -> 89 K UniProt: Stabilizes apo-protein in the D-state; Fe-S cluster assembly 3-fold slower than wild-type..
90 -> 90 N UniProt: Stabilizes apo-protein in the D-state; Fe-S cluster assembly 3-fold slower than wild-type..
99 -> 103 LPPVK

 

Classification:
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
Note(s): Note(s): ...[more].
Evidence: [EXP-IDA-PURIFIED-PROTEIN] Assay of protein purified to homogeneity
Reference(s): [1] Bonomi F., et al., 2005
[2] Bridwell-Rabb J., et al., 2012
[3] Dai Y., et al., 2012
[4] Ezraty B., et al., 2013
[5] Jaroschinsky M., et al., 2017
[6] Kim JH., et al., 2012
[7] Puglisi R., et al., 2020
[8] Wu G., et al., 2012
[9] Yan R., et al., 2015
[10] Yee N., et al., 2014
[11] Zhang Q., et al., 2020
External database links:  
ALPHAFOLD:
P0ACD4
DIP:
DIP-48025N
ECOCYC:
G7324-MONOMER
ECOLIWIKI:
b2529
INTERPRO:
IPR002871
INTERPRO:
IPR011339
MODBASE:
P0ACD4
PANTHER:
PTHR10093
PDB:
2KQK
PDB:
2L4X
PFAM:
PF01592
PRIDE:
P0ACD4
PRODB:
PRO_000023383
REFSEQ:
NP_417024
SMR:
P0ACD4
SWISSMODEL:
P0ACD4
UNIPROT:
P0ACD4


Operon      
Name: iscRSUA         
Operon arrangement:
Transcription unit        Promoter
iscRSUA


Transcriptional Regulation      
Display Regulation             
Repressed by: IscR


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right 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]


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.


RegulonDB