TARI_STRR6
ID TARI_STRR6 Reviewed; 235 AA.
AC Q8DPI2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Ribitol-5-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_02068, ECO:0000303|PubMed:19074383};
DE EC=2.7.7.40 {ECO:0000255|HAMAP-Rule:MF_02068, ECO:0000269|PubMed:19074383};
GN Name=tarI {ECO:0000255|HAMAP-Rule:MF_02068, ECO:0000303|PubMed:19074383};
GN Synonyms=yacM; OrderedLocusNames=spr1149;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH CDP,
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=R36A;
RX PubMed=19074383; DOI=10.1128/jb.01120-08;
RA Baur S., Marles-Wright J., Buckenmaier S., Lewis R.J., Vollmer W.;
RT "Synthesis of CDP-activated ribitol for teichoic acid precursors in
RT Streptococcus pneumoniae.";
RL J. Bacteriol. 191:1200-1210(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 ECO:0000269|PubMed:19074383}.
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, ECO:0000269|PubMed:19074383};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02068,
CC ECO:0000269|PubMed:19074383}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. TarI
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02068, ECO:0000305}.
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DR EMBL; AE007317; AAK99952.1; -; Genomic_DNA.
DR PIR; D98015; D98015.
DR RefSeq; NP_358742.1; NC_003098.1.
DR RefSeq; WP_000638508.1; NC_003098.1.
DR PDB; 2VSH; X-ray; 2.00 A; A/B=1-235.
DR PDB; 2VSI; X-ray; 2.75 A; A/B=1-235.
DR PDBsum; 2VSH; -.
DR PDBsum; 2VSI; -.
DR AlphaFoldDB; Q8DPI2; -.
DR SMR; Q8DPI2; -.
DR STRING; 171101.spr1149; -.
DR EnsemblBacteria; AAK99952; AAK99952; spr1149.
DR GeneID; 60233310; -.
DR KEGG; spr:spr1149; -.
DR PATRIC; fig|171101.6.peg.1247; -.
DR eggNOG; COG1211; Bacteria.
DR HOGENOM; CLU_061281_2_3_9; -.
DR OMA; TDACKIL; -.
DR BioCyc; MetaCyc:MON-20027; -.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Nucleotidyltransferase;
KW Reference proteome; Teichoic acid biosynthesis; Transferase.
FT CHAIN 1..235
FT /note="Ribitol-5-phosphate cytidylyltransferase"
FT /id="PRO_0000075632"
FT BINDING 7..10
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02068,
FT ECO:0000305|PubMed:19074383"
FT BINDING 82..88
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02068,
FT ECO:0000305|PubMed:19074383"
FT BINDING 113
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02068,
FT ECO:0000305|PubMed:19074383"
FT SITE 14
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q46893, ECO:0000255|HAMAP-
FT Rule:MF_02068"
FT SITE 22
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q46893, ECO:0000255|HAMAP-
FT Rule:MF_02068"
FT SITE 161
FT /note="Positions ribitol 5-phosphate for the nucleophilic
FT attack"
FT /evidence="ECO:0000250|UniProtKB:Q46893, ECO:0000255|HAMAP-
FT Rule:MF_02068"
FT SITE 218
FT /note="Positions ribitol 5-phosphate for the nucleophilic
FT attack"
FT /evidence="ECO:0000250|UniProtKB:Q46893, ECO:0000255|HAMAP-
FT 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
