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Reviewed, UniProtKB/Swiss-Prot P27623 (TAGD_BACSU)

Last modified June 16, 2009. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Subcellular location

Cytoplasm.

Induction

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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 129129Glycerol-3-phosphate cytidylyltransferase
PRO_0000208466

Sites

Active site141
Active site171

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
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
P27623-1 [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: 1906926] [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: 8393871] [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: 9384377] [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: 9182537] [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: 11487587] [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: 12950927] [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: 10508782] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH CTP.
+Additional computationally mapped references.

Cross-references

Sequence databases

M57497 Genomic DNA. Translation: AAA22843.1.
AL009126 Genomic DNA. Translation: CAB15591.1.
PIRA49757.
RefSeqNP_391455.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1COZX-ray2.00A/B1-129[»]
1N1DX-ray2.00A/B/C/D1-129[»]
ModBaseSearch...

Genome annotation databases

GeneID936809.
GenomeReviewsGene locus BSU35740 in contig AL009126_GR.
KEGGbsu:BSU35740.
NMPDRfig|224308.1.peg.3581.

Organism-specific databases

SubtiListBG10449. tagD. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP27623.
OMAP27623. DLLHWGH.

Enzyme and pathway databases

BioCycBSUB224308:BSU3572-MON.
MetaCyc:MON-8809.
BRENDA2.7.7.39. 150.

Family and domain databases

InterProIPR004821. Cyt_trans_rel.
IPR004820. Cytidylyltransf.
IPR006409. G3P_cytidyltrfase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PfamPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
TIGR01518. g3p_cytidyltrns. 1 hit.
ProtoNetSearch...

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: June 16, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

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

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents