Q8TGV2 · CHS5_EXODE

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).

Catalytic activity

Features

Showing features for binding site.

118852004006008001,0001,2001,4001,6001,800
TypeIDPosition(s)Description
Binding site99-106ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcell septum
Cellular Componentmyosin complex
Cellular Componentplasma membrane
Molecular Functionactin binding
Molecular FunctionATP binding
Molecular Functionchitin synthase activity
Molecular Functioncytoskeletal motor activity
Biological Processconidium formation

Keywords

Enzyme and pathway databases

Protein family/group databases

    • GT2Glycosyltransferase Family 2

Names & Taxonomy

Protein names

  • Recommended name
    Chitin synthase 5
  • EC number
  • Alternative names
    • Chitin-UDP acetyl-glucosaminyl transferase 5
    • Class-V chitin synthase 5

Gene names

    • Name
      CHS5

Organism names

Accessions

  • Primary accession
    Q8TGV2

Organism-specific databases

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Membrane
Note: Localizes to the regions of cell wall growth in an actin-dependent fashion.

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane894-914Helical
Transmembrane929-949Helical
Transmembrane1205-1225Helical
Transmembrane1599-1619Helical
Transmembrane1626-1646Helical
Transmembrane1653-1673Helical

Keywords

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).

Miscellaneous

PTM/Processing

Features

Showing features for chain, glycosylation.

Type
IDPosition(s)Description
ChainPRO_00004607901-1885Chitin synthase 5
Glycosylation219N-linked (GlcNAc...) asparagine
Glycosylation429N-linked (GlcNAc...) asparagine
Glycosylation668N-linked (GlcNAc...) asparagine
Glycosylation1043N-linked (GlcNAc...) asparagine
Glycosylation1068N-linked (GlcNAc...) asparagine
Glycosylation1462N-linked (GlcNAc...) asparagine
Glycosylation1568N-linked (GlcNAc...) asparagine
Glycosylation1759N-linked (GlcNAc...) asparagine
Glycosylation1790N-linked (GlcNAc...) asparagine

Post-translational modification

Maximal activity requires trypsin activation, suggesting a zymogenic nature.

Keywords

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).

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain1-789Myosin motor
Region601-649Disordered
Compositional bias607-647Basic and acidic residues
Region666-690Actin-binding
Region794-817Disordered
Domain957-1016Cytochrome b5 heme-binding
Domain1827-1882DEK-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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,885
  • Mass (Da)
    208,884
  • Last updated
    2005-04-26 v2
  • Checksum
    455A842ED0D426F3
MATRGNVPAHMQASLPALPAHLQSDTHITAHLASRFHVSLPTARLSSQGLICLNTFTSSTRGPNGDKEGSAMGEPEDLARRAWARLGNRAEDQAFGFFGESGSGKTTVRSHLLSSFLSFSSTPLSSKLSLAAFVFDTLTTTKTTTTQTASKAGLFYELQYDASSNNPTLIGGKLLDHRFERSRISHVPTGERSFHVLYYLLAGTSAAEKSHLGLDGHVNITTAGTGLSRSASVSHKRWRYLGHPTQMKVGINDAEGFQHFKNALRKLEFPRTEIAEICQVLAAILHIGQLEFGTGQATLTAAEESGGYSHEGGETVTVVKNRDTLAIVAAFLGLGVQDLEESLRYKTRTIHRERVTVMLDTKGARENADELATTLYSLLVTYIIESINQRVCAAEDSVANTISIVDFPGFADHSSTGSVLDQLLNNAANESLYNTCLHSIFEKTAEMLESEEVSVPATSYFDNSDAVRGLLKHGNGLLAILDDQTRRGRTDVQFLESLRKRFENKNKAITVGSATSTMPGSNFATTNLAASFTVRHYAGEVDYPVHSLVEENGDVVSGDLMNMIKATKSDFVANLFGQEALNTVSHPAEKTAIVQAQVSSKPLRMPSVSRKKHDQLRRMASRRADRSPAPQEEEPLPGTEEAKVRRTKPTATGLTQGAAAQFLSALDNITKSLTAPNVNNYFVFCLKPNDRRIANQFDSKCVRQQVQMFGIAEISQRLRTADFTIFLPFGEFLGLTNADGGVVGSDREKAQLVLDSKHWPPNEARIGNTGVFLSERCWASIALTGSQAAAYFGGDIGSPSRPDTPGHNPFSDSKARLVGSADGTPGSFYGDEAKGGGYFGSRELDAKSDAGASAFHSGDMFRNLETKEELAEKGNKKKVEEVDVVPVSSSRKRWLAIVYFLTWYLPDFAIKWIGGMKRKDVRTAWREKFAINLLIWLSCGLVVFFIIVFPELICPKQNVYSAAELSAHDGKGKHSAYVAIRGQVFDLGAFMPNHYPKIIPQSSLKKYAGVDATGLFPVQVSALCQGKDGRVDPTVQLDYTATNISGTAAVISSTDANRKYHDFRYFTNDSRPDWFYEQMIMLKANYRKGSIGYTPQYVKTLAKKSKSIAILNDRVYDFTTYNEGGRSVRAPPGEEVPSGVDTDFMDSLVVDLFTQRAGHDVTKYWNALPLDPGLRSRMQLCLDNLFFVGVTDTRNSPRCLFARYILLAVSILLCSVIGFKFFAALQFGGKNVPENLDKFVICQVPAYTEDEDSLRRAIDSAARMRYDDKRKLLIVVCDGMIIGQGNDRPTPRIVLDILGVSETVDPEPLSFESLGEGMKQHNMGKVYSGLYEVQGHIVPFMVVVKVGKPSEVSRPGNRGKRDSQMVIMRFLHRVHYNLPMSPLELEMHHQIRNIIGVNPTFYEFMLQIDADTVVAPDSATRMVSAFLRDTRLIGVCGETSLSNAKSSFITMMQVYEYYISHNLTKAFESLFGSVTCVPGCFTMYRIRAAETGKPLFVSKEIIQDYSEIRVDTLHMKNLLHLGEDRYLTTLLLKYHSKYKTKYIFHAHAWTIAPDSWKVFMSQRRRWINSTVHNLIELIPLQQLCGFCCFSMRFVVFLDLLSTVVAPVTVAYIAYLIVLLATESDVVPLTAFILLGAIYGLQAIIFILRRKWEMIGWMIVYILAMPVFSLGLPLYAFWHMDDFSWGNTRLVRGEHGKQILLSDEGKFGPDSIPKKKWEEYQAELWDAQTQRDDARSELSGYSYGTKSYLPTGSVYGGGYNDTQHLMMAPSRSASQLDMHPTPMYGGGGGHNQSRMSLAPSEMLGSQSNLMMPSGRSVADMEMSDLTGLPTDDMLLNEIRDILRTADLMTVTKKGIKQELERRFNVNLDMKRAYIGSATEAILSGQL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias607-647Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF469116
EMBL· GenBank· DDBJ
AAL79830.2
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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