TARI1_STAA8
ID TARI1_STAA8 Reviewed; 238 AA.
AC Q2G1C0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Ribitol-5-phosphate cytidylyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_02068, ECO:0000303|PubMed:15362865};
DE EC=2.7.7.40 {ECO:0000255|HAMAP-Rule:MF_02068, ECO:0000269|PubMed:15362865};
GN Name=tarI {ECO:0000303|PubMed:15362865}; OrderedLocusNames=SAOUHSC_00225;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP ENZYME KINETICS, AND PATHWAY.
RX PubMed=15362865; DOI=10.1021/bi048866v;
RA Pereira M.P., Brown E.D.;
RT "Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of
RT reductase and cytidylyltransferase activities in Haemophilus influenzae and
RT Staphylococcus aureus.";
RL Biochemistry 43:11802-11812(2004).
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:15362865}.
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:15362865};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=78.9 uM for CTP {ECO:0000269|PubMed:15362865};
CC KM=1.28 mM for D-ribitol 5-phosphate {ECO:0000269|PubMed:15362865};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02068,
CC ECO:0000305|PubMed:15362865}.
CC -!- SUBUNIT: Heterodimer together with TarJ. {ECO:0000269|PubMed:15362865}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. TarI
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02068, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000253; ABD29400.1; -; Genomic_DNA.
DR RefSeq; WP_000872486.1; NZ_LS483365.1.
DR RefSeq; YP_498820.1; NC_007795.1.
DR PDB; 6XHP; X-ray; 1.90 A; A/B=1-238.
DR PDB; 6XHQ; X-ray; 2.40 A; A/B=1-238.
DR PDB; 6XHR; X-ray; 2.10 A; A/B/C/D/E/F=1-238.
DR PDB; 6XHS; X-ray; 2.90 A; A/B/C/D/E/F=1-238.
DR PDB; 6XHT; X-ray; 1.80 A; A/B/C/D/E/F=1-238.
DR PDBsum; 6XHP; -.
DR PDBsum; 6XHQ; -.
DR PDBsum; 6XHR; -.
DR PDBsum; 6XHS; -.
DR PDBsum; 6XHT; -.
DR AlphaFoldDB; Q2G1C0; -.
DR SMR; Q2G1C0; -.
DR STRING; 1280.SAXN108_0235; -.
DR EnsemblBacteria; ABD29400; ABD29400; SAOUHSC_00225.
DR GeneID; 3920300; -.
DR KEGG; sao:SAOUHSC_00225; -.
DR PATRIC; fig|93061.5.peg.206; -.
DR eggNOG; COG1211; Bacteria.
DR HOGENOM; CLU_061281_2_3_9; -.
DR OMA; NTMMVEL; -.
DR BioCyc; MetaCyc:MON-19987; -.
DR UniPathway; UPA00790; -.
DR PRO; PR:Q2G1C0; -.
DR Proteomes; UP000008816; 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..238
FT /note="Ribitol-5-phosphate cytidylyltransferase 1"
FT /id="PRO_1000022950"
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"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6XHT"
FT TURN 14..17
FT /evidence="ECO:0007829|PDB:6XHT"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:6XHT"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6XHT"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:6XHT"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:6XHT"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:6XHT"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:6XHT"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:6XHT"
FT HELIX 84..98
FT /evidence="ECO:0007829|PDB:6XHT"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6XHT"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:6XHT"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:6XHT"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6XHT"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:6XHT"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:6XHT"
FT STRAND 163..173
FT /evidence="ECO:0007829|PDB:6XHT"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:6XHT"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:6XHT"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:6XHT"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6XHT"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:6XHT"
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
