TARI_STRPJ
ID TARI_STRPJ Reviewed; 235 AA.
AC B8ZJT5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=SPN23F11650;
OS Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=561276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700669 / Spain 23F-1;
RX PubMed=19114491; DOI=10.1128/jb.01343-08;
RA Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C.,
RA Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D.,
RA Mitchell T.J.;
RT "Role of conjugative elements in the evolution of the multidrug-resistant
RT pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL J. Bacteriol. 191:1480-1489(2009).
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; FM211187; CAR68971.1; -; Genomic_DNA.
DR RefSeq; WP_000638527.1; NC_011900.1.
DR AlphaFoldDB; B8ZJT5; -.
DR SMR; B8ZJT5; -.
DR KEGG; sne:SPN23F11650; -.
DR HOGENOM; CLU_061281_2_3_9; -.
DR OMA; TDACKIL; -.
DR UniPathway; UPA00790; -.
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_1000191072"
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; 26255 MW; 4A90F18545150386 CRC64;
MIYAGILAGG TGTRMGISNL PKQFLELGNR PILIHTIEKF VLEPSIEKIV VGVHGDWVSH
AEDLVDKYLP LYKERIIITK GGADRNTSIK KIIEAIDAYR PLTPEDIVVT HDSVRPFITL
RMIQDNIQLA QNHDAVDTVV EAVDTIVEST NGQFITDIPN RAHLYQGQTP QTFRCKDFMD
LYGSLSDEEK EILTDACKIF VIKGKDVALA KGEYSNLKIT TVTDLKIAKS MIEKD