Q8DPI6 · LICC_STRR6
- ProteinCholine-phosphate cytidylyltransferase
- GenelicC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids229 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cytidylyltransferase involved in the biosynthesis of the phosphocholine containing cell wall constituents, teichoic acid and lipoteichoic acid, which are essential for cell separation and pathogenesis (PubMed:8837483).
Catalyzes the activation of phosphocholine (P-Cho) to CDP-choline (CDP-Cho) (PubMed:11466299, PubMed:11706035, PubMed:11786295, PubMed:31420548, PubMed:8837483).
Can also use phosphoethanolamine and 2-aminoethylphosphonate, with much lower efficiency (PubMed:11466299, PubMed:31420548).
Shows lower activity with dCTP, weak activity with ATP and no activity with GTP, TTP, UTP, dATP, dGTP and dTTP (PubMed:11466299, PubMed:11786295).
Catalyzes the activation of phosphocholine (P-Cho) to CDP-choline (CDP-Cho) (PubMed:11466299, PubMed:11706035, PubMed:11786295, PubMed:31420548, PubMed:8837483).
Can also use phosphoethanolamine and 2-aminoethylphosphonate, with much lower efficiency (PubMed:11466299, PubMed:31420548).
Shows lower activity with dCTP, weak activity with ATP and no activity with GTP, TTP, UTP, dATP, dGTP and dTTP (PubMed:11466299, PubMed:11786295).
Catalytic activity
- CTP + H+ + phosphocholine = CDP-choline + diphosphateThis reaction proceeds in the forward direction.
Cofactor
Note: Kinetic data and structures suggest that the magnesium ion plays a direct role in catalysis.
Activity regulation
Mg2+ in slight excess of CTP gives maximal activity (PubMed:11786295).
Strongly inhibited by Ca2+ and several other metal ions, such as Cd2+, Co2+, Cu2+, Mn2+, Ni2+, Zn2+ and Fe2+ (PubMed:11786295).
Also inhibited by Mg2+ at high concentrations (PubMed:11786295).
CDP-Cho is a competitive inhibitor with respect to CTP, whereas diphosphate is a mixed-type inhibitor with respect to CTP (PubMed:11706035).
Strongly inhibited by Ca2+ and several other metal ions, such as Cd2+, Co2+, Cu2+, Mn2+, Ni2+, Zn2+ and Fe2+ (PubMed:11786295).
Also inhibited by Mg2+ at high concentrations (PubMed:11786295).
CDP-Cho is a competitive inhibitor with respect to CTP, whereas diphosphate is a mixed-type inhibitor with respect to CTP (PubMed:11706035).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
83 μM | phosphocholine | |||||
390 μM | phosphocholine | |||||
2.4 μM | phosphocholine | |||||
133 μM | CTP | |||||
890 μM | CTP | |||||
1.43 mM | phosphoethanolamine | |||||
300 μM | 2-aminoethylphosphonate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
7.7 μmol/min/mg | with phosphocholine or CTP as substrate | ||||
0.06 μmol/min/mg | with phosphoethanolamine as substrate | ||||
39.1 μmol/min/mg |
kcat is 17.5 sec-1 with phosphocholine as substrate (PubMed:11786295).
kcat is 1.06 sec-1 with phosphocholine as substrate. kcat is 0.72 sec-1 with 2-aminoethylphosphonate as substrate (PubMed:31420548).
kcat is 1.06 sec-1 with phosphocholine as substrate. kcat is 0.72 sec-1 with 2-aminoethylphosphonate as substrate (PubMed:31420548).
pH Dependence
Maximally active in neutral and alkaline conditions.
Pathway
Cell wall biogenesis; teichoic acid biosynthesis.
Cell wall biogenesis; lipoteichoic acid biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 6 | CDP-choline (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 8 | CDP-choline (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 9 | CDP-choline (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 80 | CDP-choline (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 82 | CDP-choline (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 85 | CDP-choline (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 101 | CDP-choline (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 102 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 185 | CDP-choline (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 211 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 213 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | nucleotidyltransferase activity | |
Biological Process | cell wall organization | |
Biological Process | lipoteichoic acid biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCholine-phosphate cytidylyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionQ8DPI6
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000459654 | 1-229 | Choline-phosphate cytidylyltransferase | |||
Sequence: MKAIILAAGLGTRLRPMTENTPKALVQVNQKPLIEYQIEFLKEKGINDIIIIVGYLKEQFDYLKEKYGVRLVFNDKYADYNNFYSLYLVKEELANSYVIDADNYLFKNMFRNDLTRSTYFSVYREDCTNEWFLVYGDDYKVQDIIVDSKAGRILSGVSFWDAPTAEKIVSFIDKAYASGEFVDLYWDNMVKDNIKELDVYVEELEGNSIYEIDSVQDYRKLEEILKNEN |
Structure
Family & Domains
Domain
The structures of apo-LicC and the LicC-CDP-choline-Mg2+ ternary complex show a significant conformational change driven by the multivalent coordination of Mg2+.
Sequence similarities
Belongs to the LicC/PntC cytidylyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length229
- Mass (Da)26,875
- Last updated2003-03-01 v1
- Checksum69DE5275F8CDDA46
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF402777 EMBL· GenBank· DDBJ | AAK94072.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE007317 EMBL· GenBank· DDBJ | AAK99948.1 EMBL· GenBank· DDBJ | Genomic DNA |