ID   TARD_BACSH              Reviewed;         129 AA.
AC   Q8RKI6; B7ZDL0; E0U4X4;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Glycerol-3-phosphate cytidylyltransferase;
DE            Short=GCT;
DE            Short=GCTase;
DE            Short=Gro-PCT;
DE            EC=2.7.7.39 {ECO:0000250|UniProtKB:P27623};
DE   AltName: Full=CDP-glycerol pyrophosphorylase;
GN   Name=tarD; OrderedLocusNames=BSUW23_17550;
OS   Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS   subtilis subsp. spizizenii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=655816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=11882717; DOI=10.1099/00221287-148-3-815;
RA   Lazarevic V., Abellan F.-X., Beggah Moeller S., Karamata D., Maueel C.;
RT   "Comparison of ribitol and glycerol teichoic acid genes in Bacillus
RT   subtilis W23 and 168: identical function, similar divergent organization,
RT   but different regulation.";
RL   Microbiology 148:815-824(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RA   Soldo B., Freymond P.P., Karamata D., Lazarevic V.;
RT   "Minor teichoic acid of Bacillus subtilis W23.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA   Zeigler D.R.;
RT   "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT   into speciation within the B. subtilis complex and into the history of B.
RT   subtilis genetics.";
RL   Microbiology 157:2033-2041(2011).
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:11882717}.
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:0000250|UniProtKB:P27623};
CC   -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC       biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P27623}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P27623}.
CC   -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR   EMBL; AJ313428; CAC86112.1; -; Genomic_DNA.
DR   EMBL; AM260209; CAJ97399.1; -; Genomic_DNA.
DR   EMBL; CP002183; ADM39545.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RKI6; -.
DR   SMR; Q8RKI6; -.
DR   EnsemblBacteria; ADM39545; ADM39545; BSUW23_17550.
DR   KEGG; bss:BSUW23_17550; -.
DR   HOGENOM; CLU_034585_2_2_9; -.
DR   OMA; VVYFPYT; -.
DR   UniPathway; UPA00790; -.
DR   Proteomes; UP000002233; 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   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Cytoplasm; Nucleotidyltransferase;
KW   Teichoic acid biosynthesis; Transferase.
FT   CHAIN           1..129
FT                   /note="Glycerol-3-phosphate cytidylyltransferase"
FT                   /id="PRO_0000208467"
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   129 AA;  15257 MW;  F2317D5F8A00247E CRC64;
     MKKVITYGTF DLFHYGHMKL LERAKNLGDY LIVGLSTDEF NLQKQKKSHH SYEHRKFILE
     TIDLVNEVIP EKNWEQKISD IQKHDIDTFV IGDDWKGKFD FLKEYCEVIY LPRTDGISTT
     QIKKDMASL