We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU00705
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00705
General rule information
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| Accession | PRU00705 |
| Dates | 14-APR-2008 (Created)
19-NOV-2022 (Last updated, Version 9) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51373; HIPIP |
Name | High potential iron-sulfur proteins family |
| Function | High potential iron-sulfur proteins (HiPIP) are a specific class of high-redox potential 4Fe-4S ferredoxins that functions in anaerobic electron transport and which occurs commonly in purple photosynthetic bacteria and in other bacteria, such as Paracoccus denitrificans and Thiobacillus ferrooxidans. |
| Scope(s) |
Bacteria |
| Example(s) | P59860; |
Propagated annotation
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Identifier, protein and gene names
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| Protein name | AltName: Full=High-potential iron-sulfur protein; Short=HiPIP; |
Comments
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| FUNCTION | Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. |
| SUBCELLULAR LOCATION | Periplasm. |
| SIMILARITY | Belongs to the high-potential iron-sulfur protein (HiPIP) family. |
Keywords
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Gene Ontology
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| GO:0051539; Molecular function:4 iron, 4 sulfur cluster binding |
| GO:0005506; Molecular function:iron ion binding |
| GO:0051536; Molecular function:iron-sulfur cluster binding |
| GO:0046872; Molecular function:metal ion binding |
| GO:0006810; Biological process:transport |
| GO:0042597; Cellular component:periplasmic space |
Features
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| From: PS51373 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 36 | 36 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | ||||||||
| BINDING | 39 | 39 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | ||||||||
| BINDING | 53 | 53 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | ||||||||
| BINDING | 67 | 67 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | ||||||||
Additional information
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| Size range | 55-90 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Not cytoplasmic |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Bacteria [24] All [ 24 ]
- Retrieve set of proteins with 3D structure for this domain