Q8TGV2 · CHS5_EXODE
- ProteinChitin synthase 5
- GeneCHS5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1885 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (PubMed:19431044).
CHS5 is required for the sustained growth at 37 degrees Celsius and is of critical importance for virulence (PubMed:14871935, PubMed:18992354).
Especially important at infection temperatures for maintaining the cell wall integrity of developing yeast buds, elongating tips of hyphae, and random sites of expansion in sclerotic forms (PubMed:18992354).
CHS5 is required for the sustained growth at 37 degrees Celsius and is of critical importance for virulence (PubMed:14871935, PubMed:18992354).
Especially important at infection temperatures for maintaining the cell wall integrity of developing yeast buds, elongating tips of hyphae, and random sites of expansion in sclerotic forms (PubMed:18992354).
Catalytic activity
- [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + UDP + H+This reaction proceeds in the forward direction.
[(1→4)-N-acetyl-β-D-glucosaminyl](n) RHEA-COMP:9593 + CHEBI:57705 = [(1→4)-N-acetyl-β-D-glucosaminyl](n+1) RHEA-COMP:9595 + CHEBI:58223 + CHEBI:15378
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 99-106 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell septum | |
Cellular Component | myosin complex | |
Cellular Component | plasma membrane | |
Molecular Function | actin binding | |
Molecular Function | ATP binding | |
Molecular Function | chitin synthase activity | |
Molecular Function | cytoskeletal motor activity | |
Biological Process | conidium formation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameChitin synthase 5
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Herpotrichiellaceae > Exophiala
Accessions
- Primary accessionQ8TGV2
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Localizes to the regions of cell wall growth in an actin-dependent fashion.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 894-914 | Helical | |||
Transmembrane | 929-949 | Helical | |||
Transmembrane | 1205-1225 | Helical | |||
Transmembrane | 1599-1619 | Helical | |||
Transmembrane | 1626-1646 | Helical | |||
Transmembrane | 1653-1673 | Helical | |||
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Leads to hyperpigmentation and loss of viability in stationary phase at 37 degrees Celsius (PubMed:14871935).
Reduces the virulence in a mouse model of acute infection (PubMed:14871935).
Causes cell wall integrity defects and subsequent abnormal yeast morphology at 37 degrees Celsius (PubMed:14871935).
Does dot lead to compensation by increased expression of another chitin synthase genes (PubMed:12213927).
Reduces the virulence in a mouse model of acute infection (PubMed:14871935).
Causes cell wall integrity defects and subsequent abnormal yeast morphology at 37 degrees Celsius (PubMed:14871935).
Does dot lead to compensation by increased expression of another chitin synthase genes (PubMed:12213927).
Miscellaneous
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000460790 | 1-1885 | Chitin synthase 5 | ||
Glycosylation | 219 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 429 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 668 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 1043 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 1068 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 1462 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 1568 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 1759 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 1790 | N-linked (GlcNAc...) asparagine | |||
Post-translational modification
Maximal activity requires trypsin activation, suggesting a zymogenic nature.
Keywords
- PTM
Expression
Induction
The expression level increases quickly and almost doubles when cells were shifted to 37 degrees Celsius, compared to cells maintained at 25 degrees Celsius (PubMed:12213927, PubMed:14871935, PubMed:17937668).
Expression is also increased under additional stress conditions that are known to initiate development of the sclerotic morphology (acidic conditions or Ca2+ limitation induced by EGTA) or of hyphae (induced by nitrogen limitation) (PubMed:14871935).
At least one negative regulator binding sequence exists in the promoter between -880 and -680 bp and another regulatory binding site is localized between bp -680 and -450 bp (PubMed:14871935).
Expression is also increased under additional stress conditions that are known to initiate development of the sclerotic morphology (acidic conditions or Ca2+ limitation induced by EGTA) or of hyphae (induced by nitrogen limitation) (PubMed:14871935).
At least one negative regulator binding sequence exists in the promoter between -880 and -680 bp and another regulatory binding site is localized between bp -680 and -450 bp (PubMed:14871935).
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 1-789 | Myosin motor | |||
Region | 601-649 | Disordered | |||
Compositional bias | 607-647 | Basic and acidic residues | |||
Region | 666-690 | Actin-binding | |||
Region | 794-817 | Disordered | |||
Domain | 957-1016 | Cytochrome b5 heme-binding | |||
Domain | 1827-1882 | DEK-C | |||
Domain
Contains an N-terminal myosin motor-like domain with a P-loop (MMD) that is involved in the actin-dependent localization to the regions of cell wall growth.
Sequence similarities
In the N-terminal section; belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
In the C-terminal section; belongs to the chitin synthase family. Class V subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,885
- Mass (Da)208,884
- Last updated2005-04-26 v2
- Checksum455A842ED0D426F3
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 607-647 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF469116 EMBL· GenBank· DDBJ | AAL79830.2 EMBL· GenBank· DDBJ | Genomic DNA |