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P27623 (TAGD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycerol-3-phosphate cytidylyltransferase

Short name=GCT
Short name=Gro-PCT
EC=2.7.7.39
Alternative name(s):
CDP-glycerol pyrophosphorylase
Teichoic acid biosynthesis protein D
Gene names
Name:tagD
Ordered Locus Names:BSU35740
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Provides activated glycerol phosphate for teichoic acid synthesis, via incorporation into both the linkage unit and the teichoic acid polymer by TagB and TagF.

Catalytic activity

CTP + sn-glycerol 3-phosphate = diphosphate + CDP-glycerol. Ref.8

Cofactor

Divalent metal cations. Prefers cobalt, magnesium, manganese or iron.

Enzyme regulation

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

Pathway

Cell wall biogenesis; poly(glucopyranosyl N-acetylgalactosamine 1-phosphate) teichoic acid biosynthesis.

Cell wall biogenesis; poly(glycerol phosphate) teichoic acid biosynthesis.

Subunit structure

Homodimer. Ref.8

Subcellular location

Cytoplasm.

Induction

Positively regulated by YycF. Mainly expressed during exponential growth and rapidly shut off as cells enter the stationary phase. Ref.6

Miscellaneous

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

Sequence similarities

Belongs to the cytidylyltransferase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 129129Glycerol-3-phosphate cytidylyltransferase
PRO_0000208466

Regions

Nucleotide binding9 – 102CTP
Nucleotide binding14 – 174CTP
Nucleotide binding113 – 1208CTP

Sites

Binding site441Substrate
Binding site461CTP
Binding site771Substrate

Experimental info

Mutagenesis111D → A or E: 0.1% of wild-type activity. Ref.4
Mutagenesis141H → A: Complete loss of activity. Ref.4
Mutagenesis171H → A: Complete loss of activity. Ref.4
Mutagenesis381D → A: 8% of wild-type activity, but 7-fold decrease in substrate affinity. Ref.4
Mutagenesis441K → A: Reduces affinity for glycerol 3-phosphate about 100-fold. Ref.8
Mutagenesis461K → A: Reduces affinity for glycerol 3-phosphate about 100-fold. Ref.8
Mutagenesis551R → A: 0.25% of wild-type activity. Ref.4
Mutagenesis551R → K: 23% of wild-type activity. Ref.4
Mutagenesis631R → A: 14% of wild-type activity. Ref.4
Mutagenesis661D → A: Complete loss of activity, and widespread change in 3D-structure. Ref.4
Mutagenesis661D → E: 16% of wild-type activity. Ref.4
Mutagenesis741W → A: 50% of wild-type activity, but 9-fold decrease in substrate affinity. Ref.4
Mutagenesis841H → A: Complete loss of activity. Ref.4
Mutagenesis941D → A: 18% of wild-type activity, but 100-fold decrease in substrate affinity. Ref.4
Mutagenesis1131R → A: 1.75% of wild-type activity. Ref.4
Mutagenesis1131R → K: Complete loss of activity. Ref.4
Mutagenesis1141T → A: 9% of wild-type activity. Ref.4
Mutagenesis1181S → A: 6% of wild-type activity. Ref.4
Mutagenesis1191T → A: 8% of wild-type activity. Ref.4

Secondary structure

......................... 129
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27623 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: B07F532D9AAE0869

FASTA12915,272
        10         20         30         40         50         60 
MKKVITYGTF DLLHWGHIKL LERAKQLGDY LVVAISTDEF NLQKQKKAYH SYEHRKLILE 

        70         80         90        100        110        120 
TIRYVDEVIP EKNWEQKKQD IIDHNIDVFV MGDDWEGKFD FLKDQCEVVY LPRTEGISTT 


KIKEEIAGL 

« Hide

References

« Hide 'large scale' references
[1]"Genes concerned with synthesis of poly(glycerol phosphate), the essential teichoic acid in Bacillus subtilis strain 168, are organized in two divergent transcription units."
Maueel C., Young M., Karamata D.
J. Gen. Microbiol. 137:929-941(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Expression, purification, and characterization of CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis."
Park Y.S., Sweitzer T.D., Dixon J.E., Kent C.
J. Biol. Chem. 268:16648-16654(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Identification of functional conserved residues of CTP:glycerol-3-phosphate cytidylyltransferase. Role of histidines in the conserved HXGH in catalysis."
Park Y.S., Gee P., Sanker S., Schurter E.J., Zuiderweg E.R., Kent C.
J. Biol. Chem. 272:15161-15166(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-11; HIS-14; HIS-17; ASP-38; ARG-55; ARG-63; ASP-66; TRP-74; HIS-84; ASP-94; ARG-113; THR-114; SER-118 AND THR-119.
[5]"Negative cooperativity of substrate binding but not enzyme activity in wild-type and mutant forms of CTP:glycerol-3-phosphate cytidylyltransferase."
Sanker S., Campbell H.A., Kent C.
J. Biol. Chem. 276:37922-37928(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MECHANISM.
[6]"Genes controlled by the essential YycG/YycF two-component system of Bacillus subtilis revealed through a novel hybrid regulator approach."
Howell A., Dubrac S., Andersen K.K., Noone D., Fert J., Msadek T., Devine K.
Mol. Microbiol. 49:1639-1655(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REGULATION BY YYCF/YYCG.
[7]"A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis."
Weber C.H., Park Y.S., Sanker S., Kent C., Ludwig M.L.
Structure 7:1113-1124(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH CTP.
[8]"Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis."
Pattridge K.A., Weber C.H., Friesen J.A., Sanker S., Kent C., Ludwig M.L.
J. Biol. Chem. 278:51863-51871(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CDP-GLYCEROL, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF LYS-44 AND LYS-46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57497 Genomic DNA. Translation: AAA22843.1.
AL009126 Genomic DNA. Translation: CAB15591.1.
PIRA49757.
RefSeqNP_391455.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1COZX-ray2.00A/B1-129[»]
1N1DX-ray2.00A/B/C/D1-129[»]
ProteinModelPortalP27623.
SMRP27623. Positions 1-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU35740.

Proteomic databases

PaxDbP27623.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15591; CAB15591; BSU35740.
GeneID936809.
KEGGbsu:BSU35740.
PATRIC18979164. VBIBacSub10457_3744.

Organism-specific databases

GenoListBSU35740. [Micado]

Phylogenomic databases

eggNOGCOG0615.
HOGENOMHOG000284153.
KOK00980.
OMASTDEFNW.
OrthoDBEOG65F90G.
ProtClustDBCLSK887975.

Enzyme and pathway databases

BioCycBSUB:BSU35740-MONOMER.
MetaCyc:MONOMER-8809.
UniPathwayUPA00789.
UPA00827.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR004821. Cyt_trans-like.
IPR006409. G3P_cytidylTrfase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
TIGR01518. g3p_cytidyltrns. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP27623.

Entry information

Entry nameTAGD_BACSU
AccessionPrimary (citable) accession number: P27623
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 13, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList