P0ACD4 · ISCU_ECOLI

  • Protein
    Iron-sulfur cluster assembly scaffold protein IscU
  • Gene
    iscU
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

A scaffold on which IscS assembles Fe-S clusters. Exists as 2 interconverting forms, a structured (S) and disordered (D) form. The D-state is the preferred substrate for IscS. Converts to the S-state when an Fe-S cluster is assembled, which helps it dissociate from IscS to transfer the Fe-S to an acceptor. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters.

Activity regulation

Carboxymethylation by iodoacetic acid blocks sulfur transfer to this protein.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular ComponentIscS-IscU complex
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functioncopper ion binding
Molecular Functionferrous iron binding
Molecular Functionidentical protein binding
Molecular Functionzinc ion binding
Biological Processintracellular iron ion homeostasis
Biological Processiron-sulfur cluster assembly
Biological ProcessL-cysteine catabolic process

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Iron-sulfur cluster assembly scaffold protein IscU
  • Alternative names
    • Sulfur acceptor protein IscU

Gene names

    • Name
      iscU
    • Synonyms
      nifU, yfhN
    • Ordered locus names
      b2529, JW2513

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0ACD4
  • Secondary accessions
    • P77310

Proteomes

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis39Stabilizes apo-protein in the S-state (structured).
Mutagenesis39No effect on equilibrium between S- and D-state (disordered).
Mutagenesis89Stabilizes apo-protein in the D-state; Fe-S cluster assembly 3-fold slower than wild-type.
Mutagenesis90Stabilizes apo-protein in the S-state; biphasic Fe-S cluster assembly 7-fold slower than wild-type.
Mutagenesis90Stabilizes apo-protein in the D-state; Fe-S cluster assembly 3-fold slower than wild-type.
Mutagenesis107Stabilizes apo-protein in the S-state; biphasic Fe-S cluster assembly 7-fold slower than wild-type.
Mutagenesis111Stabilizes apo-protein in the S-state; biphasic Fe-S cluster assembly 7-fold slower than wild-type.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001661841-128Iron-sulfur cluster assembly scaffold protein IscU

Proteomic databases

Interaction

Subunit

Homodimer. Forms a heterotetramer with IscS; each subunit of the IscS dimer contacts an IscU monomer.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P0ACD4iscS P0A6B712EBI-561646, EBI-550055
BINARY P0ACD4iscU P0ACD45EBI-561646, EBI-561646

Complex viewer

View interactors in UniProtKB
View CPX-2141 in Complex Portal

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the NifU family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    128
  • Mass (Da)
    13,849
  • Last updated
    2005-11-22 v1
  • Checksum
    47516021442B6535
MAYSEKVIDHYENPRNVGSFDNNDENVGSGMVGAPACGDVMKLQIKVNDEGIIEDARFKTYGCGSAIASSSLVTEWVKGKSLDEAQAIKNTDIAEELELPPVKIHCSILAEDAIKAAIADYKSKREAK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U00096
EMBL· GenBank· DDBJ
AAC75582.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAA16423.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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