ID   TARI_STRP2              Reviewed;         235 AA.
AC   Q04K52;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=SPD_1127;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(2007).
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}.
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DR   EMBL; CP000410; ABJ55399.1; -; Genomic_DNA.
DR   RefSeq; WP_000638508.1; NC_008533.2.
DR   AlphaFoldDB; Q04K52; -.
DR   SMR; Q04K52; -.
DR   STRING; 373153.SPD_1127; -.
DR   EnsemblBacteria; ABJ55399; ABJ55399; SPD_1127.
DR   GeneID; 60233310; -.
DR   KEGG; spd:SPD_1127; -.
DR   eggNOG; COG1211; Bacteria.
DR   HOGENOM; CLU_061281_2_3_9; -.
DR   OMA; TDACKIL; -.
DR   OrthoDB; 1836139at2; -.
DR   BioCyc; SPNE373153:G1G6V-1218-MON; -.
DR   UniPathway; UPA00790; -.
DR   Proteomes; UP000001452; 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   Teichoic acid biosynthesis; Transferase.
FT   CHAIN           1..235
FT                   /note="Ribitol-5-phosphate cytidylyltransferase"
FT                   /id="PRO_1000022951"
FT   BINDING         7..10
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   BINDING         82..88
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   BINDING         113
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            161
FT                   /note="Positions ribitol 5-phosphate for the nucleophilic
FT                   attack"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   SITE            218
FT                   /note="Positions ribitol 5-phosphate for the nucleophilic
FT                   attack"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
SQ   SEQUENCE   235 AA;  26242 MW;  0CD17F5952786D97 CRC64;
     MIYAGILAGG TGTRMGISNL PKQFLELGDR PILIHTIEKF VLEPSIEKIV VGVHGDWVSH
     AEDLVDKYLP LYKERIIITK GGADRNTSIK NIIEAIDAYR PLTPEDIVVT HDSVRPFITL
     RMIQDNIQLA QNHDAVDTVV EAVDTIVEST NGQFITDIPN RAHLYQGQTP QTFRCKDFMD
     LYGSLSDEEK EILTDACKIF VIKGKDVALA KGEYSNLKIT TVTDLKIAKS MIEKD