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Protein

Glycerol-3-phosphate cytidylyltransferase

Gene

tagD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 Publication

Catalytic activityi

CTP + sn-glycerol 3-phosphate = diphosphate + CDP-glycerol.2 Publications

Enzyme regulationi

Inhibited by the divalent cations cadmium, mercury, tin, copper and zinc.

Kineticsi

  1. KM=3.85 mM for CTP1 Publication
  2. KM=3.23 mM for glycerol 3-phosphate1 Publication
  1. 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

Pathwayi: poly(glucopyranosyl N-acetylgalactosamine 1-phosphate) teichoic acid biosynthesis

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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei44Substrate1 Publication1
Binding sitei46CTP2 Publications1
Binding sitei77Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi9 – 10CTP2 Publications2
Nucleotide bindingi14 – 17CTP2 Publications4
Nucleotide bindingi113 – 120CTP2 Publications8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionNucleotidyltransferase, Transferase
Biological processCell wall biogenesis/degradation, Teichoic acid biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU35740-MONOMER.
MetaCyc:MONOMER-8809.
BRENDAi2.7.7.39. 658.
UniPathwayiUPA00789.
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
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi11D → A or E: 0.1% of wild-type activity. 1 Publication1
Mutagenesisi14H → A: Complete loss of activity. 1 Publication1
Mutagenesisi17H → A: Complete loss of activity. 1 Publication1
Mutagenesisi38D → A: 8% of wild-type activity, but 7-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi44K → A: Reduces affinity for glycerol 3-phosphate about 100-fold. 1 Publication1
Mutagenesisi46K → A: Reduces affinity for glycerol 3-phosphate about 100-fold. 1 Publication1
Mutagenesisi55R → A: 0.25% of wild-type activity. 1 Publication1
Mutagenesisi55R → K: 23% of wild-type activity. 1 Publication1
Mutagenesisi63R → A: 14% of wild-type activity. 1 Publication1
Mutagenesisi66D → A: Complete loss of activity, and widespread change in 3D-structure. 1 Publication1
Mutagenesisi66D → E: 16% of wild-type activity. 1 Publication1
Mutagenesisi74W → A: 50% of wild-type activity, but 9-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi84H → A: Complete loss of activity. 1 Publication1
Mutagenesisi94D → A: 18% of wild-type activity, but 100-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi113R → A: 1.75% of wild-type activity. 1 Publication1
Mutagenesisi113R → K: Complete loss of activity. 1 Publication1
Mutagenesisi114T → A: 9% of wild-type activity. 1 Publication1
Mutagenesisi118S → A: 6% of wild-type activity. 1 Publication1
Mutagenesisi119T → A: 8% of wild-type activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002084661 – 129Glycerol-3-phosphate cytidylyltransferaseAdd BLAST129

Proteomic databases

PaxDbiP27623.

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 Publications

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019336.

Structurei

Secondary structure

1129
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi15 – 25Combined sources11
Beta strandi28 – 36Combined sources9
Helixi38 – 44Combined sources7
Helixi52 – 59Combined sources8
Beta strandi67 – 71Combined sources5
Helixi74 – 76Combined sources3
Helixi77 – 83Combined sources7
Beta strandi87 – 92Combined sources6
Helixi93 – 95Combined sources3
Turni96 – 99Combined sources4
Helixi100 – 102Combined sources3
Turni103 – 105Combined sources3
Beta strandi106 – 111Combined sources6
Helixi119 – 124Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1COZX-ray2.00A/B1-129[»]
1N1DX-ray2.00A/B/C/D1-129[»]
ProteinModelPortaliP27623.
SMRiP27623.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27623.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytidylyltransferase family.Curated

Phylogenomic databases

eggNOGiENOG4107ZIC. Bacteria.
COG0615. LUCA.
HOGENOMiHOG000284153.
InParanoidiP27623.
KOiK00980.
OMAiVMGNDWE.
PhylomeDBiP27623.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiView protein in InterPro
IPR004821. Cyt_trans-like.
IPR006409. G3P_cytidylTrfase.
IPR014729. Rossmann-like_a/b/a_fold.
PfamiView protein in Pfam
PF01467. CTP_transf_like. 1 hit.
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR01518. g3p_cytidyltrns. 1 hit.

Sequencei

Sequence statusi: Complete.

P27623-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:129
Mass (Da):15,272
Last modified:August 1, 1992 - v1
Checksum:iB07F532D9AAE0869
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57497 Genomic DNA. Translation: AAA22843.1.
AL009126 Genomic DNA. Translation: CAB15591.1.
PIRiA49757.
RefSeqiNP_391455.1. NC_000964.3.
WP_003227921.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15591; CAB15591; BSU35740.
GeneIDi936809.
KEGGibsu:BSU35740.
PATRICi18979164. VBIBacSub10457_3744.

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.
PIRiA49757.
RefSeqiNP_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 entryMethodResolution (Å)ChainPositionsPDBsum
1COZX-ray2.00A/B1-129[»]
1N1DX-ray2.00A/B/C/D1-129[»]
ProteinModelPortaliP27623.
SMRiP27623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019336.

Proteomic databases

PaxDbiP27623.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15591; CAB15591; BSU35740.
GeneIDi936809.
KEGGibsu:BSU35740.
PATRICi18979164. VBIBacSub10457_3744.

Phylogenomic databases

eggNOGiENOG4107ZIC. Bacteria.
COG0615. LUCA.
HOGENOMiHOG000284153.
InParanoidiP27623.
KOiK00980.
OMAiVMGNDWE.
PhylomeDBiP27623.

Enzyme and pathway databases

UniPathwayiUPA00789.
UPA00827.
BioCyciBSUB:BSU35740-MONOMER.
MetaCyc:MONOMER-8809.
BRENDAi2.7.7.39. 658.

Miscellaneous databases

EvolutionaryTraceiP27623.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiView protein in InterPro
IPR004821. Cyt_trans-like.
IPR006409. G3P_cytidylTrfase.
IPR014729. Rossmann-like_a/b/a_fold.
PfamiView protein in Pfam
PF01467. CTP_transf_like. 1 hit.
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR01518. g3p_cytidyltrns. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTAGD_BACSU
AccessioniPrimary (citable) accession number: P27623
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 18, 2017
This is version 147 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Proceeds via a random order reaction mechanism where there is negative cooperativity in the binding of substrates but not in catalysis.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.