TARI_LISMF
ID TARI_LISMF Reviewed; 237 AA.
AC Q720Y7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ribitol-5-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_02068};
DE EC=2.7.7.40 {ECO:0000255|HAMAP-Rule:MF_02068};
GN Name=tarI {ECO:0000255|HAMAP-Rule:MF_02068};
GN OrderedLocusNames=LMOf2365_1100;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(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 -!- 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; AE017262; AAT03877.1; -; Genomic_DNA.
DR RefSeq; WP_003724626.1; NC_002973.6.
DR PDB; 3F1C; X-ray; 2.30 A; A/B=2-236.
DR PDBsum; 3F1C; -.
DR AlphaFoldDB; Q720Y7; -.
DR SMR; Q720Y7; -.
DR DNASU; 2799328; -.
DR KEGG; lmf:LMOf2365_1100; -.
DR HOGENOM; CLU_061281_2_3_9; -.
DR OMA; TDACKIL; -.
DR UniPathway; UPA00790; -.
DR EvolutionaryTrace; Q720Y7; -.
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_0000075586"
FT BINDING 7..10
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT BINDING 80..86
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 159
FT /note="Positions ribitol 5-phosphate for the nucleophilic
FT attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT SITE 216
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:3F1C"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:3F1C"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3F1C"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:3F1C"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:3F1C"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3F1C"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:3F1C"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3F1C"
FT HELIX 83..97
FT /evidence="ECO:0007829|PDB:3F1C"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3F1C"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:3F1C"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:3F1C"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3F1C"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:3F1C"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:3F1C"
FT STRAND 162..172
FT /evidence="ECO:0007829|PDB:3F1C"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:3F1C"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:3F1C"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:3F1C"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:3F1C"
FT HELIX 220..233
FT /evidence="ECO:0007829|PDB:3F1C"
SQ SEQUENCE 237 AA; 26793 MW; 72A1EEA5300BE053 CRC64;
MIYAQILAGG KGTRMGNVSM PKQFLPLNGK PIIVHTVEKF ILNTRFDKIL ISSPKEWMNH
AEDNIKKYIS DDRIVVIEGG EDRNETIMNG IRFVEKTYGL TDDDIIVTHD AVRPFLTHRI
IEENIDAALE TGAVDTVIEA LDTIVESSNH EVITDIPVRD HMYQGQTPQS FNMKKVFNHY
QNLTPEKKQI LTDACKICLL AGDDVKLVKG EIFNIKITTP YDLKVANAII QERIAND
