ID   TARI_LACPL              Reviewed;         233 AA.
AC   Q88W46; F9UPF9;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Ribitol-5-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_02068};
DE            EC=2.7.7.40 {ECO:0000255|HAMAP-Rule:MF_02068};
GN   Name=tarI {ECO:0000255|HAMAP-Rule:MF_02068}; OrderedLocusNames=lp_1816;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
CC   -!- FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to D-
CC       ribitol 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_02068}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + D-ribitol 5-phosphate + H(+) = CDP-L-ribitol +
CC         diphosphate; Xref=Rhea:RHEA:12456, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57608,
CC         ChEBI:CHEBI:57695; EC=2.7.7.40; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02068};
CC   -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02068}.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. TarI
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_02068}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL935263; CCC79098.1; -; Genomic_DNA.
DR   RefSeq; WP_011101561.1; NC_004567.2.
DR   RefSeq; YP_004889612.1; NC_004567.2.
DR   AlphaFoldDB; Q88W46; -.
DR   SMR; Q88W46; -.
DR   STRING; 220668.lp_1816; -.
DR   EnsemblBacteria; CCC79098; CCC79098; lp_1816.
DR   KEGG; lpl:lp_1816; -.
DR   PATRIC; fig|220668.9.peg.1534; -.
DR   eggNOG; COG1211; Bacteria.
DR   HOGENOM; CLU_061281_2_3_9; -.
DR   OMA; TDACKIL; -.
DR   PhylomeDB; Q88W46; -.
DR   BioCyc; LPLA220668:G1GW0-1561-MON; -.
DR   UniPathway; UPA00790; -.
DR   Proteomes; UP000000432; Chromosome.
DR   GO; GO:0047349; F:D-ribitol-5-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:1902012; P:poly(ribitol phosphate) teichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02516; CDP-ME_synthetase; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_02068; TarI; 1.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR018294; ISPD_synthase_CS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR034709; TarI.
DR   Pfam; PF01128; IspD; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   PROSITE; PS01295; ISPD; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Nucleotidyltransferase;
KW   Reference proteome; Teichoic acid biosynthesis; Transferase.
FT   CHAIN           1..233
FT                   /note="Ribitol-5-phosphate cytidylyltransferase"
FT                   /id="PRO_0000075580"
FT   BINDING         7..10
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   BINDING         80..86
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   SITE            14
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   SITE            22
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   SITE            158
FT                   /note="Positions ribitol 5-phosphate for the nucleophilic
FT                   attack"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   SITE            215
FT                   /note="Positions ribitol 5-phosphate for the nucleophilic
FT                   attack"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
SQ   SEQUENCE   233 AA;  25901 MW;  6A576C790713C0D7 CRC64;
     MIYAQILAGG KGTRMGNVPM PKQFLLLADK PILIHTIEKF TLESRFDAIL VVCPADWVSH
     TEDIIKKYIT DERVHVVVGG ADRNETLMSG INYIQDHYGI QDDDVVVTHD AVRPFITQRI
     INDNIVAVLE NKAVDTVVPA IDTIVRGAND QVTDIPVRSE MYQGQTPQSF HIKILIDSYN
     ALSSEQKASL SDSCKICSLA GQKVSLVRGE NYNFKITTPF DLRVASALVE KRS