TARI_BACSH
ID TARI_BACSH Reviewed; 237 AA.
AC Q8RKI9; B7ZDK7; E0U4X7;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ribitol-5-phosphate cytidylyltransferase {ECO:0000250|UniProtKB:Q8DPI2, ECO:0000255|HAMAP-Rule:MF_02068};
DE EC=2.7.7.40 {ECO:0000250|UniProtKB:Q8DPI2, ECO:0000255|HAMAP-Rule:MF_02068};
GN Name=tarI {ECO:0000255|HAMAP-Rule:MF_02068, ECO:0000303|PubMed:11882717};
GN Synonyms=ispD; OrderedLocusNames=BSUW23_17565;
OS Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS subtilis subsp. spizizenii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=655816;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PUTATIVE FUNCTION.
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=11882717; DOI=10.1099/00221287-148-3-815;
RA Lazarevic V., Abellan F.-X., Beggah Moeller S., Karamata D., Maueel C.;
RT "Comparison of ribitol and glycerol teichoic acid genes in Bacillus
RT subtilis W23 and 168: identical function, similar divergent organization,
RT but different regulation.";
RL Microbiology 148:815-824(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RA Soldo B., Freymond P.P., Karamata D., Lazarevic V.;
RT "Minor teichoic acid of Bacillus subtilis W23.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA Zeigler D.R.;
RT "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT into speciation within the B. subtilis complex and into the history of B.
RT subtilis genetics.";
RL Microbiology 157:2033-2041(2011).
CC -!- FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to D-
CC ribitol 5-phosphate. {ECO:0000250|UniProtKB:Q8DPI2, ECO:0000255|HAMAP-
CC 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;
CC Evidence={ECO:0000250|UniProtKB:Q8DPI2, 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 ECO:0000303|PubMed:11882717}.
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; AJ313428; CAC86109.1; -; Genomic_DNA.
DR EMBL; AM260209; CAJ97396.1; -; Genomic_DNA.
DR EMBL; CP002183; ADM39548.1; -; Genomic_DNA.
DR PDB; 4JIS; X-ray; 1.77 A; A/B=1-237.
DR PDBsum; 4JIS; -.
DR AlphaFoldDB; Q8RKI9; -.
DR SMR; Q8RKI9; -.
DR EnsemblBacteria; ADM39548; ADM39548; BSUW23_17565.
DR KEGG; bss:BSUW23_17565; -.
DR HOGENOM; CLU_061281_2_3_9; -.
DR OMA; TDACKIL; -.
DR BioCyc; MetaCyc:MON-19969; -.
DR BRENDA; 2.7.7.40; 658.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000002233; 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 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Nucleotidyltransferase;
KW Teichoic acid biosynthesis; Transferase.
FT CHAIN 1..237
FT /note="Ribitol-5-phosphate cytidylyltransferase"
FT /id="PRO_0000075685"
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 BINDING 112
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:4JIS"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:4JIS"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:4JIS"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:4JIS"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:4JIS"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:4JIS"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:4JIS"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4JIS"
FT HELIX 84..98
FT /evidence="ECO:0007829|PDB:4JIS"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4JIS"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:4JIS"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:4JIS"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:4JIS"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:4JIS"
FT STRAND 163..173
FT /evidence="ECO:0007829|PDB:4JIS"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:4JIS"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:4JIS"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:4JIS"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:4JIS"
SQ SEQUENCE 237 AA; 26848 MW; 0B03F2F41D6CE5AB CRC64;
MIYAEILAGG KGSRMGNVNM PKQFLPLNKR PIIIHTVEKF LLNDRFDKIL IVSPKEWINH
TKDILKKFIG QDDRLVVVEG GSDRNESIMS GIRYIEKEFG IQDNDVIITH DSVRPFLTHR
IIDENIDAVL QYGAVDTVIS AIDTIIASED QEFISDIPVR DNMYQGQTPQ SFRISKLVEL
YNKLSDEQKA VLTDACKICS LAGEKVKLVR GEVFNIKVTT PYDLKVANAI LQERISQ
