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TARI_STRA5
ID   TARI_STRA5              Reviewed;         240 AA.
AC   Q8DYQ7;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SAG1417;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; AE009948; AAN00287.1; -; Genomic_DNA.
DR   RefSeq; NP_688414.1; NC_004116.1.
DR   RefSeq; WP_000981011.1; NC_004116.1.
DR   AlphaFoldDB; Q8DYQ7; -.
DR   SMR; Q8DYQ7; -.
DR   STRING; 208435.SAG1417; -.
DR   EnsemblBacteria; AAN00287; AAN00287; SAG1417.
DR   GeneID; 66886295; -.
DR   KEGG; sag:SAG1417; -.
DR   PATRIC; fig|208435.3.peg.1425; -.
DR   HOGENOM; CLU_061281_2_3_9; -.
DR   OMA; VCKSGWE; -.
DR   UniPathway; UPA00790; -.
DR   Proteomes; UP000000821; 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..240
FT                   /note="Ribitol-5-phosphate cytidylyltransferase"
FT                   /id="PRO_0000075628"
FT   BINDING         8..11
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   BINDING         81..87
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   SITE            15
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   SITE            23
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   240 AA;  26487 MW;  54A62031A9B76293 CRC64;
     MMNIGVIFAG GVGRRMNTKG KPKQFLEVHG KPIIVHTIDI FQNTEAIDAV VVVCVSDWLD
     YMNNLVERFN LTKVKAVVAG GETGQMSIFK GLEAAEQLAT DDAVVLIHDG VRPLINEEVI
     NANIQSVKET GSAVTSVRAK ETVVLVNDSS KISEVVDRTR SFIAKAPQSF YLSDILSVER
     DAISKGITDA IDSSTLMGMY NRELTIVEGP YENIKITTPD DFYMFKALYD ARENEQIYGM
 
 
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