TARI2_STAA8
ID TARI2_STAA8 Reviewed; 238 AA.
AC Q2G2C4;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ribitol-5-phosphate cytidylyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_02068, ECO:0000305};
DE EC=2.7.7.40 {ECO:0000255|HAMAP-Rule:MF_02068, ECO:0000269|PubMed:18556787};
GN Name=tarI' {ECO:0000303|PubMed:18556787};
GN OrderedLocusNames=SAOUHSC_00220 {ECO:0000312|EMBL:ABD29396.1};
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, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBUNIT.
RC STRAIN=RN4220;
RX PubMed=18556787; DOI=10.1128/jb.00526-08;
RA Pereira M.P., D'Elia M.A., Troczynska J., Brown E.D.;
RT "Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus
RT leads to functionally redundant poly(ribitol phosphate) polymerases.";
RL J. Bacteriol. 190:5642-5649(2008).
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:18556787}.
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:18556787};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38.7 uM for CTP {ECO:0000269|PubMed:18556787};
CC KM=102.2 uM for D-ribitol 5-phosphate {ECO:0000269|PubMed:18556787};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02068,
CC ECO:0000269|PubMed:18556787}.
CC -!- SUBUNIT: Heterodimer together with TarJ. {ECO:0000269|PubMed:18556787}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. TarI
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02068, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD29396.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000253; ABD29396.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000638475.1; NZ_LS483365.1.
DR RefSeq; YP_498815.1; NC_007795.1.
DR AlphaFoldDB; Q2G2C4; -.
DR SMR; Q2G2C4; -.
DR STRING; 1280.SAXN108_0230; -.
DR EnsemblBacteria; ABD29396; ABD29396; SAOUHSC_00220.
DR GeneID; 3920296; -.
DR KEGG; sao:SAOUHSC_00220; -.
DR PATRIC; fig|93061.5.peg.202; -.
DR eggNOG; COG1211; Bacteria.
DR HOGENOM; CLU_061281_2_3_9; -.
DR SABIO-RK; Q2G2C4; -.
DR UniPathway; UPA00790; -.
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 Cell wall biogenesis/degradation; Nucleotidyltransferase;
KW Reference proteome; Teichoic acid biosynthesis; Transferase.
FT CHAIN 1..238
FT /note="Ribitol-5-phosphate cytidylyltransferase 2"
FT /id="PRO_0000437479"
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; 26575 MW; A2C4EB712DFC764E CRC64;
MIYAGILAGG IGSRMGNVPL PKQFLDIDNK PILIHTIEKF ILVSEFNEII IATPAQWISH
TQDILKKYNI TDQRVKVVAG GTDRNETIMN IIDHIRNVNG INNDDVIVTH DAVRPFLTQR
IIKENIEVAA KYGAVDTVIE AIDTIVMSKD KQNIHSIPVR NEMYQGQTPQ SFNIKLLQDS
YRALSSEQKE ILSDACKIIV ESGHAVKLVR GELYNIKVTT PYDLKVANAI IQGDIADD
