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P27623

- TAGD_BACSU

UniProt

P27623 - TAGD_BACSU

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
  1. 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. teichoic acid biosynthetic process Source: UniProtKB-KW

    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-SubCell

    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.
    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

    MKKVITYGTF DLLHWGHIKL LERAKQLGDY LVVAISTDEF NLQKQKKAYH    50
    SYEHRKLILE TIRYVDEVIP EKNWEQKKQD IIDHNIDVFV MGDDWEGKFD 100
    FLKDQCEVVY LPRTEGISTT KIKEEIAGL 129
    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.
    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

    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 1, 2014
    This is version 131 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