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UniProtKB - P27623 (TAGD_BACSU)
Protein
Glycerol-3-phosphate cytidylyltransferase
Gene
tagD
Organism
Bacillus subtilis (strain 168)
Status
Functioni
Catalyzes the transfer of the cytidylyl group of CTP to sn-glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit and the teichoic acid polymer by TagB and TagF.
1 PublicationMiscellaneous
Proceeds via a random order reaction mechanism where there is negative cooperativity in the binding of substrates but not in catalysis.
Catalytic activityi
- EC:2.7.7.392 Publications
Activity regulationi
Inhibited by the divalent cations cadmium, mercury, tin, copper and zinc.
Kineticsi
- KM=3.85 mM for CTP1 Publication
- KM=3.23 mM for glycerol 3-phosphate1 Publication
- Vmax=185 µmol/min/mg enzyme1 Publication
pH dependencei
Optimum pH is 6.5-9.5.1 Publication
Temperature dependencei
Optimum temperature is 50 degrees Celsius.1 Publication
: poly(glucopyranosyl N-acetylgalactosamine 1-phosphate) teichoic acid biosynthesis Pathwayi
This protein is involved in the pathway poly(glucopyranosyl N-acetylgalactosamine 1-phosphate) teichoic acid biosynthesis, which is part of Cell wall biogenesis.View all proteins of this organism that are known to be involved in the pathway poly(glucopyranosyl N-acetylgalactosamine 1-phosphate) teichoic acid biosynthesis and in Cell wall biogenesis.
Pathwayi: poly(glycerol phosphate) teichoic acid biosynthesis
This protein is involved in the pathway poly(glycerol phosphate) teichoic acid biosynthesis, which is part of Cell wall biogenesis.View all proteins of this organism that are known to be involved in the pathway poly(glycerol phosphate) teichoic acid biosynthesis and in Cell wall biogenesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 44 | Substrate1 Publication | 1 | |
Binding sitei | 46 | CTP2 Publications | 1 | |
Binding sitei | 77 | Substrate1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 9 – 10 | CTP2 Publications | 2 | |
Nucleotide bindingi | 14 – 17 | CTP2 Publications | 4 | |
Nucleotide bindingi | 113 – 120 | CTP2 Publications | 8 |
GO - Molecular functioni
- glycerol-3-phosphate cytidylyltransferase activity Source: UniProtKB-EC
- metal ion binding Source: InterPro
GO - Biological processi
- cell wall organization Source: UniProtKB-KW
- teichoic acid biosynthetic process Source: UniProtKB-KW
Keywordsi
Molecular function | Nucleotidyltransferase, Transferase |
Biological process | Cell wall biogenesis/degradation, Teichoic acid biosynthesis |
Enzyme and pathway databases
BioCyci | BSUB:BSU35740-MONOMER |
BRENDAi | 2.7.7.39, 658 |
UniPathwayi | UPA00789 UPA00827 |
Names & Taxonomyi
Protein namesi | Recommended name: Glycerol-3-phosphate cytidylyltransferase1 Publication (EC:2.7.7.392 Publications)Short name: GCT Short name: GCTase1 Publication Short name: Gro-PCT Alternative name(s): CDP-glycerol pyrophosphorylase Teichoic acid biosynthesis protein D |
Gene namesi | Name:tagD1 Publication Ordered Locus Names:BSU35740 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 11 | D → A or E: 0.1% of wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 14 | H → A: Complete loss of activity. 1 Publication | 1 | |
Mutagenesisi | 17 | H → A: Complete loss of activity. 1 Publication | 1 | |
Mutagenesisi | 38 | D → A: 8% of wild-type activity, but 7-fold decrease in substrate affinity. 1 Publication | 1 | |
Mutagenesisi | 44 | K → A: Reduces affinity for glycerol 3-phosphate about 100-fold. 1 Publication | 1 | |
Mutagenesisi | 46 | K → A: Reduces affinity for glycerol 3-phosphate about 100-fold. 1 Publication | 1 | |
Mutagenesisi | 55 | R → A: 0.25% of wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 55 | R → K: 23% of wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 63 | R → A: 14% of wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 66 | D → A: Complete loss of activity, and widespread change in 3D-structure. 1 Publication | 1 | |
Mutagenesisi | 66 | D → E: 16% of wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 74 | W → A: 50% of wild-type activity, but 9-fold decrease in substrate affinity. 1 Publication | 1 | |
Mutagenesisi | 84 | H → A: Complete loss of activity. 1 Publication | 1 | |
Mutagenesisi | 94 | D → A: 18% of wild-type activity, but 100-fold decrease in substrate affinity. 1 Publication | 1 | |
Mutagenesisi | 113 | R → A: 1.75% of wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 113 | R → K: Complete loss of activity. 1 Publication | 1 | |
Mutagenesisi | 114 | T → A: 9% of wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 118 | S → A: 6% of wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 119 | T → A: 8% of wild-type activity. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB02484, Cytidine 5'-diphosphoglycerol DB02431, Cytidine-5'-Triphosphate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000208466 | 1 – 129 | Glycerol-3-phosphate cytidylyltransferaseAdd BLAST | 129 |
Proteomic databases
jPOSTi | P27623 |
PaxDbi | P27623 |
Expressioni
Inductioni
Positively regulated by WalR. Mainly expressed during exponential growth and rapidly shut off as cells enter the stationary phase.
Interactioni
Subunit structurei
Homodimer.
2 PublicationsProtein-protein interaction databases
STRINGi | 224308.BSU35740 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P27623 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P27623 |
Family & Domainsi
Sequence similaritiesi
Belongs to the cytidylyltransferase family.Curated
Phylogenomic databases
eggNOGi | COG0615, Bacteria |
InParanoidi | P27623 |
OMAi | VVYFPYT |
PhylomeDBi | P27623 |
Family and domain databases
Gene3Di | 3.40.50.620, 1 hit |
InterProi | View protein in InterPro IPR004821, Cyt_trans-like IPR006409, G3P_cytidylTrfase IPR014729, Rossmann-like_a/b/a_fold |
Pfami | View protein in Pfam PF01467, CTP_transf_like, 1 hit |
TIGRFAMsi | TIGR00125, cyt_tran_rel, 1 hit TIGR01518, g3p_cytidyltrns, 1 hit |
i Sequence
Sequence statusi: Complete.
P27623-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKKVITYGTF DLLHWGHIKL LERAKQLGDY LVVAISTDEF NLQKQKKAYH
60 70 80 90 100
SYEHRKLILE TIRYVDEVIP EKNWEQKKQD IIDHNIDVFV MGDDWEGKFD
110 120
FLKDQCEVVY LPRTEGISTT KIKEEIAGL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M57497 Genomic DNA Translation: AAA22843.1 AL009126 Genomic DNA Translation: CAB15591.1 |
PIRi | A49757 |
RefSeqi | NP_391455.1, NC_000964.3 WP_003227921.1, NZ_JNCM01000034.1 |
Genome annotation databases
EnsemblBacteriai | CAB15591; CAB15591; BSU_35740 |
GeneIDi | 936809 |
KEGGi | bsu:BSU35740 |
PATRICi | fig|224308.179.peg.3869 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M57497 Genomic DNA Translation: AAA22843.1 AL009126 Genomic DNA Translation: CAB15591.1 |
PIRi | A49757 |
RefSeqi | NP_391455.1, NC_000964.3 WP_003227921.1, NZ_JNCM01000034.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1COZ | X-ray | 2.00 | A/B | 1-129 | [»] | |
1N1D | X-ray | 2.00 | A/B/C/D | 1-129 | [»] | |
SMRi | P27623 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU35740 |
Chemistry databases
DrugBanki | DB02484, Cytidine 5'-diphosphoglycerol DB02431, Cytidine-5'-Triphosphate |
Proteomic databases
jPOSTi | P27623 |
PaxDbi | P27623 |
Genome annotation databases
EnsemblBacteriai | CAB15591; CAB15591; BSU_35740 |
GeneIDi | 936809 |
KEGGi | bsu:BSU35740 |
PATRICi | fig|224308.179.peg.3869 |
Phylogenomic databases
eggNOGi | COG0615, Bacteria |
InParanoidi | P27623 |
OMAi | VVYFPYT |
PhylomeDBi | P27623 |
Enzyme and pathway databases
UniPathwayi | UPA00789 UPA00827 |
BioCyci | BSUB:BSU35740-MONOMER |
BRENDAi | 2.7.7.39, 658 |
Miscellaneous databases
EvolutionaryTracei | P27623 |
Family and domain databases
Gene3Di | 3.40.50.620, 1 hit |
InterProi | View protein in InterPro IPR004821, Cyt_trans-like IPR006409, G3P_cytidylTrfase IPR014729, Rossmann-like_a/b/a_fold |
Pfami | View protein in Pfam PF01467, CTP_transf_like, 1 hit |
TIGRFAMsi | TIGR00125, cyt_tran_rel, 1 hit TIGR01518, g3p_cytidyltrns, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | TAGD_BACSU | |
Accessioni | P27623Primary (citable) accession number: P27623 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
Last sequence update: | August 1, 1992 | |
Last modified: | February 23, 2022 | |
This is version 166 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families