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P27623

- TAGD_BACSU

UniProt

P27623 - TAGD_BACSU

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Protein

Glycerol-3-phosphate cytidylyltransferase

Gene

tagD

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

Functioni

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 activityi

CTP + sn-glycerol 3-phosphate = diphosphate + CDP-glycerol.1 Publication

Cofactori

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

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441Substrate
Binding sitei46 – 461CTP
Binding sitei77 – 771Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 102CTP
Nucleotide bindingi14 – 174CTP
Nucleotide bindingi113 – 1208CTP

GO - Molecular functioni

  1. glycerol-3-phosphate cytidylyltransferase activity Source: UniProtKB-EC
  2. metal ion binding Source: InterPro

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. teichoic acid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation, Teichoic acid biosynthesis

Keywords - Ligandi

Cobalt, Iron, Magnesium, Manganese

Enzyme and pathway databases

BioCyciBSUB:BSU35740-MONOMER.
MetaCyc:MONOMER-8809.
UniPathwayiUPA00789.
UPA00827.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate cytidylyltransferase (EC:2.7.7.39)
Short name:
GCT
Short name:
Gro-PCT
Alternative name(s):
CDP-glycerol pyrophosphorylase
Teichoic acid biosynthesis protein D
Gene namesi
Name:tagD
Ordered Locus Names:BSU35740
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU35740. [Micado]

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111D → A or E: 0.1% of wild-type activity. 1 Publication
Mutagenesisi14 – 141H → A: Complete loss of activity. 1 Publication
Mutagenesisi17 – 171H → A: Complete loss of activity. 1 Publication
Mutagenesisi38 – 381D → A: 8% of wild-type activity, but 7-fold decrease in substrate affinity. 1 Publication
Mutagenesisi44 – 441K → A: Reduces affinity for glycerol 3-phosphate about 100-fold. 1 Publication
Mutagenesisi46 – 461K → A: Reduces affinity for glycerol 3-phosphate about 100-fold. 1 Publication
Mutagenesisi55 – 551R → A: 0.25% of wild-type activity. 1 Publication
Mutagenesisi55 – 551R → K: 23% of wild-type activity. 1 Publication
Mutagenesisi63 – 631R → A: 14% of wild-type activity. 1 Publication
Mutagenesisi66 – 661D → A: Complete loss of activity, and widespread change in 3D-structure. 1 Publication
Mutagenesisi66 – 661D → E: 16% of wild-type activity. 1 Publication
Mutagenesisi74 – 741W → A: 50% of wild-type activity, but 9-fold decrease in substrate affinity. 1 Publication
Mutagenesisi84 – 841H → A: Complete loss of activity. 1 Publication
Mutagenesisi94 – 941D → A: 18% of wild-type activity, but 100-fold decrease in substrate affinity. 1 Publication
Mutagenesisi113 – 1131R → A: 1.75% of wild-type activity. 1 Publication
Mutagenesisi113 – 1131R → K: Complete loss of activity. 1 Publication
Mutagenesisi114 – 1141T → A: 9% of wild-type activity. 1 Publication
Mutagenesisi118 – 1181S → A: 6% of wild-type activity. 1 Publication
Mutagenesisi119 – 1191T → A: 8% of wild-type activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 129129Glycerol-3-phosphate cytidylyltransferasePRO_0000208466Add
BLAST

Proteomic databases

PaxDbiP27623.

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224308.BSU35740.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86
Helixi15 – 2511
Beta strandi28 – 369
Helixi38 – 447
Helixi52 – 598
Beta strandi67 – 715
Helixi74 – 763
Helixi77 – 837
Beta strandi87 – 926
Helixi93 – 953
Turni96 – 994
Helixi100 – 1023
Turni103 – 1053
Beta strandi106 – 1116
Helixi119 – 1246

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1COZX-ray2.00A/B1-129[»]
1N1DX-ray2.00A/B/C/D1-129[»]
ProteinModelPortaliP27623.
SMRiP27623. Positions 1-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27623.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytidylyltransferase family.Curated

Phylogenomic databases

eggNOGiCOG0615.
HOGENOMiHOG000284153.
InParanoidiP27623.
KOiK00980.
OMAiKKTYFSY.
OrthoDBiEOG65F90G.
PhylomeDBiP27623.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR006409. G3P_cytidylTrfase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
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:
EMBL
GenBank
DDBJ
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_CM000487.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_CM000487.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P27623.
SMRi P27623. Positions 1-126.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU35740.

Proteomic databases

PaxDbi P27623.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15591 ; CAB15591 ; BSU35740 .
GeneIDi 936809.
KEGGi bsu:BSU35740.
PATRICi 18979164. VBIBacSub10457_3744.

Organism-specific databases

GenoListi BSU35740. [Micado ]

Phylogenomic databases

eggNOGi COG0615.
HOGENOMi HOG000284153.
InParanoidi P27623.
KOi K00980.
OMAi KKTYFSY.
OrthoDBi EOG65F90G.
PhylomeDBi P27623.

Enzyme and pathway databases

UniPathwayi UPA00789 .
UPA00827 .
BioCyci BSUB:BSU35740-MONOMER.
MetaCyc:MONOMER-8809.

Miscellaneous databases

EvolutionaryTracei P27623.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
InterProi IPR004821. Cyt_trans-like.
IPR006409. G3P_cytidylTrfase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
Pfami PF01467. CTP_transf_2. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00125. cyt_tran_rel. 1 hit.
TIGR01518. g3p_cytidyltrns. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTAGD_BACSU
AccessioniPrimary (citable) accession number: P27623
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 29, 2014
This is version 132 of the entry and version 1 of the sequence. [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, 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

External Data

Dasty 3