TARD_STAA8
ID TARD_STAA8 Reviewed; 132 AA.
AC Q2G2X2;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Glycerol-3-phosphate cytidylyltransferase {ECO:0000305};
DE Short=GCT {ECO:0000305};
DE Short=GCTase {ECO:0000305};
DE Short=Gro-PCT {ECO:0000305};
DE EC=2.7.7.39 {ECO:0000269|PubMed:12637027};
DE AltName: Full=CDP-glycerol pyrophosphorylase {ECO:0000305};
GN Name=tarD {ECO:0000303|PubMed:12637027};
GN OrderedLocusNames=SAOUHSC_00645 {ECO:0000312|EMBL:ABD29780.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47 {ECO:0000312|Proteomes:UP000008816};
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, REACTION MECHANISM, AND ENZYME KINETICS.
RX PubMed=12637027; DOI=10.1016/s1570-9639(03)00019-0;
RA Badurina D.S., Zolli-Juran M., Brown E.D.;
RT "CTP:glycerol 3-phosphate cytidylyltransferase (TarD) from Staphylococcus
RT aureus catalyzes the cytidylyl transfer via an ordered Bi-Bi reaction
RT mechanism with micromolar K(m) values.";
RL Biochim. Biophys. Acta 1646:196-206(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS), AND SUBUNIT.
RX PubMed=16344011; DOI=10.1016/j.bbapap.2005.10.015;
RA Fong D.H., Yim V.C.-N., D'Elia M.A., Brown E.D., Berghuis A.M.;
RT "Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from
RT Staphylococcus aureus: examination of structural basis for kinetic
RT mechanism.";
RL Biochim. Biophys. Acta 1764:63-69(2006).
CC -!- FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to sn-
CC glycerol 3-phosphate so the activated glycerol 3-phosphate can be used
CC for teichoic acid synthesis, via incorporation into both the linkage
CC unit by TarB and TarF. {ECO:0000269|PubMed:12637027}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + sn-glycerol 3-phosphate = CDP-glycerol +
CC diphosphate; Xref=Rhea:RHEA:13361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:58311; EC=2.7.7.39;
CC Evidence={ECO:0000269|PubMed:12637027};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for CTP {ECO:0000269|PubMed:12637027};
CC KM=21 uM for glycerol 3-phosphate {ECO:0000269|PubMed:12637027};
CC Note=kcat is 2.6 sec(-1). {ECO:0000269|PubMed:12637027};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000305|PubMed:12637027}.
CC -!- SUBUNIT: Homotetramer or homodimer. {ECO:0000269|PubMed:12637027,
CC ECO:0000269|PubMed:16344011}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P27623}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; CP000253; ABD29780.1; -; Genomic_DNA.
DR RefSeq; WP_000832260.1; NZ_LS483365.1.
DR RefSeq; YP_499205.1; NC_007795.1.
DR PDB; 2B7L; X-ray; 3.00 A; A/B/C/D=1-132.
DR PDBsum; 2B7L; -.
DR AlphaFoldDB; Q2G2X2; -.
DR SMR; Q2G2X2; -.
DR STRING; 1280.SAXN108_0709; -.
DR EnsemblBacteria; ABD29780; ABD29780; SAOUHSC_00645.
DR GeneID; 3919937; -.
DR GeneID; 66838933; -.
DR KEGG; sao:SAOUHSC_00645; -.
DR eggNOG; COG0615; Bacteria.
DR HOGENOM; CLU_034585_2_2_9; -.
DR OMA; VVYFPYT; -.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047348; F:glycerol-3-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR006409; G3P_cytidylTrfase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR TIGRFAMs; TIGR01518; g3p_cytidyltrns; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Cytoplasm;
KW Nucleotidyltransferase; Reference proteome; Teichoic acid biosynthesis;
KW Transferase.
FT CHAIN 1..132
FT /note="Glycerol-3-phosphate cytidylyltransferase"
FT /id="PRO_0000438714"
FT BINDING 9..10
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P27623"
FT BINDING 14..17
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P27623"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27623"
FT BINDING 46
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P27623"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27623"
FT BINDING 113..120
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P27623"
SQ SEQUENCE 132 AA; 15817 MW; AB836BA24663EF30 CRC64;
MKRVITYGTY DLLHYGHIEL LRRAREMGDY LIVALSTDEF NQIKHKKSYY DYEQRKMMLE
SIRYVDLVIP EKGWGQKEDD VEKFDVDVFV MGHDWEGEFD FLKDKCEVIY LKRTEGISTT
KIKQELYGKD AK
