ID   TARI1_STAAC             Reviewed;         238 AA.
AC   Q5HJC1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Ribitol-5-phosphate cytidylyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_02068};
DE            EC=2.7.7.40 {ECO:0000255|HAMAP-Rule:MF_02068};
GN   Name=tarI1 {ECO:0000255|HAMAP-Rule:MF_02068}; OrderedLocusNames=SACOL0240;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW38795.1; -; Genomic_DNA.
DR   RefSeq; WP_000872486.1; NC_002951.2.
DR   AlphaFoldDB; Q5HJC1; -.
DR   SMR; Q5HJC1; -.
DR   EnsemblBacteria; AAW38795; AAW38795; SACOL0240.
DR   KEGG; sac:SACOL0240; -.
DR   HOGENOM; CLU_061281_2_3_9; -.
DR   OMA; NTMMVEL; -.
DR   UniPathway; UPA00790; -.
DR   Proteomes; UP000000530; 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..238
FT                   /note="Ribitol-5-phosphate cytidylyltransferase 1"
FT                   /id="PRO_0000075614"
FT   BINDING         7..10
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            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            160
FT                   /note="Positions ribitol 5-phosphate for the nucleophilic
FT                   attack"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   SITE            217
FT                   /note="Positions ribitol 5-phosphate for the nucleophilic
FT                   attack"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
SQ   SEQUENCE   238 AA;  26657 MW;  B19F7EA82D847A0F CRC64;
     MKYAGILAGG IGSRMGNVPL PKQFLDLDNK PILIHTLEKF ILINDFEKII IATPQQWMTH
     TKDTLRKFKI SDERIEVIQG GSDRNDTIMN IVKHIESTNG INDDDVIVTH DAVRPFLTHR
     IIKENIQAAL EYGAVDTVID AIDTIVTSKD NQTIDAIPVR NEMYQGQTPQ SFNINLLKES
     YAQLSDEQKS ILSDACKIIV ETNKPVRLVK GELYNIKVTT PYDLKVANAI IRGGIADD