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Glycerol-3-phosphate cytidylyltransferase (GCT) (GCTase) (Gro-PCT) (EC 2.7.7.39) (CDP-glycerol pyrophosphorylase) (Teichoic acid biosynthesis protein D)

 TAGD_BACSU              Reviewed;         129 AA.
P27623;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
07-JUN-2017, entry version 149.
RecName: Full=Glycerol-3-phosphate cytidylyltransferase {ECO:0000303|PubMed:8393871};
Short=GCT;
Short=GCTase {ECO:0000303|PubMed:8393871};
Short=Gro-PCT;
EC=2.7.7.39 {ECO:0000269|PubMed:14506262, ECO:0000269|PubMed:8393871};
AltName: Full=CDP-glycerol pyrophosphorylase;
AltName: Full=Teichoic acid biosynthesis protein D;
Name=tagD {ECO:0000303|PubMed:8393871}; OrderedLocusNames=BSU35740;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=1906926; DOI=10.1099/00221287-137-4-929;
Maueel C., Young M., Karamata D.;
"Genes concerned with synthesis of poly(glycerol phosphate), the
essential teichoic acid in Bacillus subtilis strain 168, are organized
in two divergent transcription units.";
J. Gen. Microbiol. 137:929-941(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
SPECIFICITY, AND SUBCELLULAR LOCATION.
STRAIN=168 / BR151;
PubMed=8393871;
Park Y.S., Sweitzer T.D., Dixon J.E., Kent C.;
"Expression, purification, and characterization of CTP:glycerol-3-
phosphate cytidylyltransferase from Bacillus subtilis.";
J. Biol. Chem. 268:16648-16654(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
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.
PubMed=9182537; DOI=10.1074/jbc.272.24.15161;
Park Y.S., Gee P., Sanker S., Schurter E.J., Zuiderweg E.R., Kent C.;
"Identification of functional conserved residues of CTP:glycerol-3-
phosphate cytidylyltransferase. Role of histidines in the conserved
HXGH in catalysis.";
J. Biol. Chem. 272:15161-15166(1997).
[5]
REACTION MECHANISM.
PubMed=11487587; DOI=10.1074/jbc.M107198200;
Sanker S., Campbell H.A., Kent C.;
"Negative cooperativity of substrate binding but not enzyme activity
in wild-type and mutant forms of CTP:glycerol-3-phosphate
cytidylyltransferase.";
J. Biol. Chem. 276:37922-37928(2001).
[6]
REGULATION BY WALR/WALK.
PubMed=12950927; DOI=10.1046/j.1365-2958.2003.03661.x;
Howell A., Dubrac S., Andersen K.K., Noone D., Fert J., Msadek T.,
Devine K.;
"Genes controlled by the essential YycG/YycF two-component system of
Bacillus subtilis revealed through a novel hybrid regulator
approach.";
Mol. Microbiol. 49:1639-1655(2003).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH CTP.
PubMed=10508782; DOI=10.1016/S0969-2126(99)80178-6;
Weber C.H., Park Y.S., Sanker S., Kent C., Ludwig M.L.;
"A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate
cytidylyltransferase from Bacillus subtilis.";
Structure 7:1113-1124(1999).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CDP-GLYCEROL,
CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF LYS-44 AND LYS-46.
PubMed=14506262; DOI=10.1074/jbc.M306174200;
Pattridge K.A., Weber C.H., Friesen J.A., Sanker S., Kent C.,
Ludwig M.L.;
"Glycerol-3-phosphate cytidylyltransferase. Structural changes induced
by binding of CDP-glycerol and the role of lysine residues in
catalysis.";
J. Biol. Chem. 278:51863-51871(2003).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:8393871}.
-!- CATALYTIC ACTIVITY: CTP + sn-glycerol 3-phosphate = diphosphate +
CDP-glycerol. {ECO:0000269|PubMed:14506262,
ECO:0000269|PubMed:8393871}.
-!- ENZYME REGULATION: Inhibited by the divalent cations cadmium,
mercury, tin, copper and zinc.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.85 mM for CTP {ECO:0000269|PubMed:8393871};
KM=3.23 mM for glycerol 3-phosphate
{ECO:0000269|PubMed:8393871};
Vmax=185 umol/min/mg enzyme {ECO:0000269|PubMed:8393871};
pH dependence:
Optimum pH is 6.5-9.5. {ECO:0000269|PubMed:8393871};
Temperature dependence:
Optimum temperature is 50 degrees Celsius.
{ECO:0000269|PubMed:8393871};
-!- PATHWAY: Cell wall biogenesis; poly(glucopyranosyl N-
acetylgalactosamine 1-phosphate) teichoic acid biosynthesis.
-!- PATHWAY: Cell wall biogenesis; poly(glycerol phosphate) teichoic
acid biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14506262,
ECO:0000269|PubMed:8393871}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000303|PubMed:8393871}.
-!- INDUCTION: Positively regulated by WalR. 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.
-!- SIMILARITY: Belongs to the cytidylyltransferase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M57497; AAA22843.1; -; Genomic_DNA.
EMBL; AL009126; CAB15591.1; -; Genomic_DNA.
PIR; A49757; A49757.
RefSeq; NP_391455.1; NC_000964.3.
RefSeq; WP_003227921.1; NZ_JNCM01000034.1.
PDB; 1COZ; X-ray; 2.00 A; A/B=1-129.
PDB; 1N1D; X-ray; 2.00 A; A/B/C/D=1-129.
PDBsum; 1COZ; -.
PDBsum; 1N1D; -.
ProteinModelPortal; P27623; -.
SMR; P27623; -.
STRING; 224308.Bsubs1_010100019336; -.
DrugBank; DB02484; Cytidine 5'-Diphosphoglycerol.
DrugBank; DB02431; Cytidine-5'-Triphosphate.
PaxDb; P27623; -.
EnsemblBacteria; CAB15591; CAB15591; BSU35740.
GeneID; 936809; -.
KEGG; bsu:BSU35740; -.
PATRIC; fig|224308.179.peg.3869; -.
eggNOG; ENOG4107ZIC; Bacteria.
eggNOG; COG0615; LUCA.
HOGENOM; HOG000284153; -.
InParanoid; P27623; -.
KO; K00980; -.
OMA; VMGNDWE; -.
PhylomeDB; P27623; -.
BioCyc; BSUB:BSU35740-MONOMER; -.
BioCyc; MetaCyc:MONOMER-8809; -.
BRENDA; 2.7.7.39; 658.
UniPathway; UPA00789; -.
UniPathway; UPA00827; -.
EvolutionaryTrace; P27623; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0047348; F:glycerol-3-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:InterPro.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-KW.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR004821; Cyt_trans-like.
InterPro; IPR006409; G3P_cytidylTrfase.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF01467; CTP_transf_like; 1.
TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
TIGRFAMs; TIGR01518; g3p_cytidyltrns; 1.
1: Evidence at protein level;
3D-structure; Cell wall biogenesis/degradation; Complete proteome;
Cytoplasm; Direct protein sequencing; Nucleotidyltransferase;
Reference proteome; Teichoic acid biosynthesis; Transferase.
CHAIN 1 129 Glycerol-3-phosphate
cytidylyltransferase.
/FTId=PRO_0000208466.
NP_BIND 9 10 CTP. {ECO:0000269|PubMed:10508782,
ECO:0000269|PubMed:14506262}.
NP_BIND 14 17 CTP. {ECO:0000269|PubMed:10508782,
ECO:0000269|PubMed:14506262}.
NP_BIND 113 120 CTP. {ECO:0000269|PubMed:10508782,
ECO:0000269|PubMed:14506262}.
BINDING 44 44 Substrate. {ECO:0000269|PubMed:14506262}.
BINDING 46 46 CTP. {ECO:0000269|PubMed:10508782,
ECO:0000269|PubMed:14506262}.
BINDING 77 77 Substrate. {ECO:0000269|PubMed:14506262}.
MUTAGEN 11 11 D->A,E: 0.1% of wild-type activity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 14 14 H->A: Complete loss of activity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 17 17 H->A: Complete loss of activity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 38 38 D->A: 8% of wild-type activity, but 7-
fold decrease in substrate affinity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 44 44 K->A: Reduces affinity for glycerol 3-
phosphate about 100-fold.
{ECO:0000269|PubMed:14506262}.
MUTAGEN 46 46 K->A: Reduces affinity for glycerol 3-
phosphate about 100-fold.
{ECO:0000269|PubMed:14506262}.
MUTAGEN 55 55 R->A: 0.25% of wild-type activity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 55 55 R->K: 23% of wild-type activity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 63 63 R->A: 14% of wild-type activity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 66 66 D->A: Complete loss of activity, and
widespread change in 3D-structure.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 66 66 D->E: 16% of wild-type activity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 74 74 W->A: 50% of wild-type activity, but 9-
fold decrease in substrate affinity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 84 84 H->A: Complete loss of activity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 94 94 D->A: 18% of wild-type activity, but 100-
fold decrease in substrate affinity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 113 113 R->A: 1.75% of wild-type activity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 113 113 R->K: Complete loss of activity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 114 114 T->A: 9% of wild-type activity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 118 118 S->A: 6% of wild-type activity.
{ECO:0000269|PubMed:9182537}.
MUTAGEN 119 119 T->A: 8% of wild-type activity.
{ECO:0000269|PubMed:9182537}.
STRAND 3 8 {ECO:0000244|PDB:1COZ}.
HELIX 15 25 {ECO:0000244|PDB:1COZ}.
STRAND 28 36 {ECO:0000244|PDB:1COZ}.
HELIX 38 44 {ECO:0000244|PDB:1COZ}.
HELIX 52 59 {ECO:0000244|PDB:1COZ}.
STRAND 67 71 {ECO:0000244|PDB:1COZ}.
HELIX 74 76 {ECO:0000244|PDB:1N1D}.
HELIX 77 83 {ECO:0000244|PDB:1COZ}.
STRAND 87 92 {ECO:0000244|PDB:1COZ}.
HELIX 93 95 {ECO:0000244|PDB:1COZ}.
TURN 96 99 {ECO:0000244|PDB:1COZ}.
HELIX 100 102 {ECO:0000244|PDB:1COZ}.
TURN 103 105 {ECO:0000244|PDB:1COZ}.
STRAND 106 111 {ECO:0000244|PDB:1COZ}.
HELIX 119 124 {ECO:0000244|PDB:1COZ}.
SEQUENCE 129 AA; 15272 MW; B07F532D9AAE0869 CRC64;
MKKVITYGTF DLLHWGHIKL LERAKQLGDY LVVAISTDEF NLQKQKKAYH SYEHRKLILE
TIRYVDEVIP EKNWEQKKQD IIDHNIDVFV MGDDWEGKFD FLKDQCEVVY LPRTEGISTT
KIKEEIAGL


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