Q4WM22 · SITA_ASPFU
- ProteinSerine/threonine-protein phosphatase sitA
- GenesitA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids388 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Protein phosphatase that acts as a modulator of pkcA/mpkA activity involved in the cell wall integrity pathway (PubMed:25911225).
Plays an important role in regulation of adhesion, cell wall integrity, biofilm formation, and virulence (PubMed:25911225).
Plays an important role in regulation of adhesion, cell wall integrity, biofilm formation, and virulence (PubMed:25911225).
Catalytic activity
- O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate
Cofactor
Note: Binds 2 manganese ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 67 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 69 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 161 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 161 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 193 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Active site | 194 | Proton donor | |||
Binding site | 243 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 317 | Mn2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | cytoplasm | |
Cellular Component | protein phosphatase type 2A complex | |
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | protein serine/threonine phosphatase activity | |
Biological Process | cell adhesion involved in biofilm formation | |
Biological Process | cellular response to oxidative stress | |
Biological Process | DNA repair | |
Biological Process | fungal-type cell wall organization | |
Biological Process | G1/S transition of mitotic cell cycle | |
Biological Process | intracellular signal transduction | |
Biological Process | negative regulation of isopentenyl diphosphate biosynthetic process, mevalonate pathway | |
Biological Process | regulation of actin cytoskeleton organization | |
Biological Process | regulation of fungal-type cell wall organization | |
Biological Process | regulation of TORC1 signaling | |
Biological Process | tRNA wobble uridine modification |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein phosphatase sitA
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionQ4WM22
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Leads to decreased mpkA phosphorylation levels, increased sensitivity to cell wall-damaging agents, increased levels of beta-(1,3)-glucan and chitin, impaired in biofilm formation, and decreased protein kinase C activity (PubMed:25911225).
Increases also sensitivity to several metals and ions, such as MnCl2, CaCl2, and LiCl, but it is more resistant to ZnSO4 (PubMed:25911225).
Impeairs the virulencein a murine model of invasive pulmonary aspergillosis and induces an augmented tumor necrosis factor alpha response in mouse macrophages (PubMed:25911225).
Increases also sensitivity to several metals and ions, such as MnCl2, CaCl2, and LiCl, but it is more resistant to ZnSO4 (PubMed:25911225).
Impeairs the virulencein a murine model of invasive pulmonary aspergillosis and induces an augmented tumor necrosis factor alpha response in mouse macrophages (PubMed:25911225).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000453182 | 1-388 | Serine/threonine-protein phosphatase sitA | ||
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 86-146 | Disordered | |||
Compositional bias | 95-109 | Polar residues | |||
Compositional bias | 111-127 | Basic and acidic residues | |||
Compositional bias | 128-143 | Polar residues | |||
Sequence similarities
Belongs to the PPP phosphatase family. PP-6 (PP-V) subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length388
- Mass (Da)43,535
- Last updated2007-04-17 v2
- Checksum931FB3CFA3E16037
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 95-109 | Polar residues | |||
Compositional bias | 111-127 | Basic and acidic residues | |||
Compositional bias | 128-143 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAHF01000006 EMBL· GenBank· DDBJ | EAL88992.2 EMBL· GenBank· DDBJ | Genomic DNA |