Q6GA85 (ISDA_STAAS) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 60.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Iron-regulated surface determinant protein A Alternative name(s): Fur-regulated protein A Staphylococcal transferrin-binding protein A | ||||||
| Gene names |
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| Organism | Staphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 282459 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 350 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Transfers its hemin to hemin-free IsdC (apo-IsdC) directly probably through the activated holo-IsdA-apo-IsdC complex and driven by the higher affinity of apo-IsdC for the cofactor. The reaction is reversible. Binds transferrin, lactoferrin, heme, hemoglobin, hemin, fetuin, asialofetuin and protein A. Also binds fibronectin and chains B-beta and gamma of fibrinogen. Could play a role in the removal of heme from hemoglobin. The IsdA-mediated iron-acquisition system from transferrin could play only an ancillary role in the iron uptake whereas the siderophore-mediated iron-acquisition system from transferrin seems to play an essential or dominant role. May function as a reservoir for heme. Involved in adherence of S.aureus to human desquamated nasal epithelial cells and is required for nasal colonization. Protects S.aureus against the bactericidal protease activity of apolactoferrin in vitro and confers resistance to bovine lactoferricin. Also IsdA and/or IsdB promote resistance to hydrogen peroxide and killing by neutrophils By similarity. |
| Subunit structure | Monomer. Interacts with IsdC By similarity. |
| Subcellular location | Secreted › cell wall; Peptidoglycan-anchor Probable. |
| Induction | Repressed by fur in the presence of iron By similarity. |
| Domain | The NEAT domain is responsible for binding Fe3+ and Fe2+ heme and fibrinogen. The NEAT domain is an inhibitor of apolactoferrin activity, while the C-domain confers resistance to bovine lactoferricin By similarity. |
| Sequence similarities | Contains 1 NEAT domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell wall Secreted |
| Domain | Signal |
| Ligand | Heme Iron Metal-binding |
| PTM | Peptidoglycan-anchor |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Cellular_component | cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular regionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 46 | 46 | By similarity | ||||||
| Chain | 47 – 316 | 270 | Iron-regulated surface determinant protein A | PRO_0000046092 | |||||
| Propeptide | 317 – 350 | 34 | Removed by sortase A Potential | PRO_0000046093 | |||||
Regions | |||||||||
| Domain | 62 – 184 | 123 | NEAT | ||||||
| Motif | 313 – 317 | 5 | LPXTG sorting signal Potential | ||||||
Sites | |||||||||
| Metal binding | 166 | 1 | Iron (heme axial ligand) By similarity | ||||||
| Binding site | 75 | 1 | Heme By similarity | ||||||
| Binding site | 82 | 1 | Heme By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 316 | 1 | Pentaglycyl murein peptidoglycan amidated threonine Potential | ||||||
Sequences
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References
| [1] | "Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. Parkhill J.Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MSSA476. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX571857 Genomic DNA. Translation: CAG42838.1. |
| RefSeq | YP_043188.1. NC_002953.3. |
3D structure databases | |
| ProteinModelPortal | Q6GA85. |
| SMR | Q6GA85. Positions 63-184. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 282459.SAS1064. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2864366. |
| KEGG | sas:SAS1064. |
| PATRIC | 19551571. VBIStaAur96780_1103. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG5386. |
| HOGENOM | HOG000107381. |
| KO | K14193. |
| OMA | TTVVNDD. |
| ProtClustDB | CLSK885153. |
Family and domain databases | |
| InterPro | IPR019948. Gram-positive_anchor. IPR019931. LPXTG-motif_cell_wall_anchor. IPR006635. NEA_transpt. [Graphical view] |
| Pfam | PF00746. Gram_pos_anchor. 1 hit. PF05031. NEAT. 1 hit. [Graphical view] |
| SMART | SM00725. NEAT. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01167. LPXTG_anchor. 1 hit. |
| PROSITE | PS50847. GRAM_POS_ANCHORING. 1 hit. PS50978. NEAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ISDA_STAAS | ||||||||
| Accession | Primary (citable) accession number: Q6GA85 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
