P77667 · SUFA_ECOLI
- ProteinIron-sulfur cluster assembly protein SufA
- GenesufA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids122 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Member of gene cluster sufABCDSE that mediates iron-sulfur cluster assembly under oxidative stress and iron limitation conditions (PubMed:17941825).
Binds [2Fe-2S] and [4Fe-4S] clusters by mobilizing sulfur atoms provided by the SufS-SufE cysteine desulfurase system and then transfers the assembled Fe-S clusters to target proteins including ferredoxin and aconitase (PubMed:17350000, PubMed:19366265).
Seems to act as a Fe-S cluster carrier rather than a scaffold, this role being performed by SufB and SufC (PubMed:19810706, PubMed:23018275).
Binds [2Fe-2S] and [4Fe-4S] clusters by mobilizing sulfur atoms provided by the SufS-SufE cysteine desulfurase system and then transfers the assembled Fe-S clusters to target proteins including ferredoxin and aconitase (PubMed:17350000, PubMed:19366265).
Seems to act as a Fe-S cluster carrier rather than a scaffold, this role being performed by SufB and SufC (PubMed:19810706, PubMed:23018275).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 50 | [2Fe-2S] cluster (UniProtKB | ChEBI); sulfuration is probably achieved via an internal sulfur transfer from C-114 or C-116 | |||
Binding site | 50 | [4Fe-4S] cluster (UniProtKB | ChEBI); sulfuration is probably achieved via an internal sulfur transfer from C-114 or C-116 | |||
Binding site | 114 | [2Fe-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 114 | [4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 116 | [2Fe-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 116 | [4Fe-4S] cluster (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | iron-sulfur cluster transfer complex | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | iron-sulfur cluster assembly | |
Biological Process | protein maturation by iron-sulfur cluster transfer | |
Biological Process | response to oxidative stress |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIron-sulfur cluster assembly protein SufA
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP77667
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Deletion has only a mild effect on cell growth (PubMed:17941825).
However, deletion of both IscA and SufA results in a severe growth phenotype in minimal medium under aerobic growth conditions (PubMed:17941825).
However, deletion of both IscA and SufA results in a severe growth phenotype in minimal medium under aerobic growth conditions (PubMed:17941825).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 50 | Decrease of sulfur binding activity. | |||
Mutagenesis | 114 | Strong decrease of sulfur binding activity. | |||
Mutagenesis | 116 | Strong decrease of sulfur binding activity. | |||
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | P77667 | sufB P77522 | 5 | EBI-1125011, EBI-562758 | |
BINARY | P77667 | sufC P77499 | 5 | EBI-1125011, EBI-561601 |
Complex viewer
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length122
- Mass (Da)13,300
- Last updated1997-02-01 v1
- MD5 Checksum03AE0C2783E02563669BDFA97CA19A67
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U00096 EMBL· GenBank· DDBJ | AAC74754.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA15453.1 EMBL· GenBank· DDBJ | Genomic DNA |