TARI1_STAAM
ID TARI1_STAAM Reviewed; 238 AA.
AC Q99WW8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=SAV0255;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB56417.1; -; Genomic_DNA.
DR RefSeq; WP_000872486.1; NC_002758.2.
DR AlphaFoldDB; Q99WW8; -.
DR SMR; Q99WW8; -.
DR World-2DPAGE; 0002:Q99WW8; -.
DR PaxDb; Q99WW8; -.
DR EnsemblBacteria; BAB56417; BAB56417; SAV0255.
DR KEGG; sav:SAV0255; -.
DR HOGENOM; CLU_061281_2_3_9; -.
DR OMA; NTMMVEL; -.
DR PhylomeDB; Q99WW8; -.
DR BioCyc; SAUR158878:SAV_RS01445-MON; -.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000002481; 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_0000075616"
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
