(data stored in ACNUC9435 zone)

SWISSPROT: TARI_LISIN

ID   TARI_LISIN              Reviewed;         237 AA.
AC   Q92CV0;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 89.
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}; OrderedLocusNames=lin1071;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(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}.
DR   EMBL; AL596167; CAC96302.1; -; Genomic_DNA.
DR   PIR; AF1566; AF1566.
DR   RefSeq; WP_003766398.1; NC_003212.1.
DR   SMR; Q92CV0; -.
DR   STRING; 272626.lin1071; -.
DR   EnsemblBacteria; CAC96302; CAC96302; CAC96302.
DR   KEGG; lin:lin1071; -.
DR   eggNOG; ENOG4108QHG; Bacteria.
DR   eggNOG; COG1211; LUCA.
DR   HOGENOM; HOG000218563; -.
DR   KO; K21030; -.
DR   OMA; TDACKIL; -.
DR   OrthoDB; 1836139at2; -.
DR   BioCyc; GCF_000195795:LIN_RS05465-MONOMER; -.
DR   UniPathway; UPA00790; -.
DR   Proteomes; UP000002513; 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;
DR   PRODOM; Q92CV0.
DR   SWISS-2DPAGE; Q92CV0.
KW   Cell wall biogenesis/degradation; Nucleotidyltransferase;
KW   Teichoic acid biosynthesis; Transferase.
FT   CHAIN           1..237
FT                   /note="Ribitol-5-phosphate cytidylyltransferase"
FT                   /id="PRO_0000075584"
FT   NP_BIND         7..10
FT                   /note="CTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02068"
FT   NP_BIND         80..86
FT                   /note="CTP"
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"
SQ   SEQUENCE   237 AA;  26848 MW;  DE41EB43F718A630 CRC64;
     MIYAQILAGG KGTRMGNVSM PKQFLPLNGK PIIVHTVEKF ILNTRFDKIL ISSPKEWMNH
     AEDNIKKYIS DDRIVVIEGG EDRNETIMNG IRYVEKTFGL NDEDIIVTHD AVRPFLTHRI
     IEENIDAAIE TGAVDTVIEA LDTIVESSNH EFITDIPVRD QMYQGQTPQS FNMKKVYNHY
     QNLSAEKKQI LTDACKICLL AGDQVKLVKG EIFNIKITTP YDLKVANAII QERIAND
//

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