P0ACD4 · ISCU_ECOLI
- ProteinIron-sulfur cluster assembly scaffold protein IscU
- GeneiscU
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids128 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | IscS-IscU complex | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | copper ion binding | |
Molecular Function | ferrous iron binding | |
Molecular Function | identical protein binding | |
Molecular Function | zinc ion binding | |
Biological Process | intracellular iron ion homeostasis | |
Biological Process | iron-sulfur cluster assembly | |
Biological Process | L-cysteine catabolic process |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIron-sulfur cluster assembly scaffold protein IscU
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0ACD4
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 39 | Stabilizes apo-protein in the S-state (structured). | ||||
Sequence: D → A, L, or V | ||||||
Mutagenesis | 39 | No effect on equilibrium between S- and D-state (disordered). | ||||
Sequence: D → G | ||||||
Mutagenesis | 89 | Stabilizes apo-protein in the D-state; Fe-S cluster assembly 3-fold slower than wild-type. | ||||
Sequence: K → A | ||||||
Mutagenesis | 90 | Stabilizes apo-protein in the S-state; biphasic Fe-S cluster assembly 7-fold slower than wild-type. | ||||
Sequence: N → A | ||||||
Mutagenesis | 90 | Stabilizes apo-protein in the D-state; Fe-S cluster assembly 3-fold slower than wild-type. | ||||
Sequence: N → D | ||||||
Mutagenesis | 107 | Stabilizes apo-protein in the S-state; biphasic Fe-S cluster assembly 7-fold slower than wild-type. | ||||
Sequence: S → A | ||||||
Mutagenesis | 111 | Stabilizes apo-protein in the S-state; biphasic Fe-S cluster assembly 7-fold slower than wild-type. | ||||
Sequence: E → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000166184 | 1-128 | Iron-sulfur cluster assembly scaffold protein IscU | |||
Sequence: MAYSEKVIDHYENPRNVGSFDNNDENVGSGMVGAPACGDVMKLQIKVNDEGIIEDARFKTYGCGSAIASSSLVTEWVKGKSLDEAQAIKNTDIAEELELPPVKIHCSILAEDAIKAAIADYKSKREAK |
Proteomic databases
Interaction
Subunit
Homodimer. Forms a heterotetramer with IscS; each subunit of the IscS dimer contacts an IscU monomer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P0ACD4 | iscS P0A6B7 | 12 | EBI-561646, EBI-550055 | |
BINARY | P0ACD4 | iscU P0ACD4 | 5 | EBI-561646, EBI-561646 |
Complex viewer
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length128
- Mass (Da)13,849
- Last updated2005-11-22 v1
- Checksum47516021442B6535
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U00096 EMBL· GenBank· DDBJ | AAC75582.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA16423.1 EMBL· GenBank· DDBJ | Genomic DNA |