ID G5JJT0_9STAP Unreviewed; 238 AA.
AC G5JJT0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Ribitol-5-phosphate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_02068};
DE EC=2.7.7.40 {ECO:0000256|HAMAP-Rule:MF_02068};
GN Name=ispD {ECO:0000313|EMBL:EHJ07587.1};
GN Synonyms=tarI {ECO:0000256|HAMAP-Rule:MF_02068};
GN ORFNames=SS7213T_08697 {ECO:0000313|EMBL:EHJ07587.1};
OS Staphylococcus simiae CCM 7213 = CCUG 51256.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=911238 {ECO:0000313|EMBL:EHJ07587.1, ECO:0000313|Proteomes:UP000005413};
RN [1] {ECO:0000313|EMBL:EHJ07587.1, ECO:0000313|Proteomes:UP000005413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 7213 {ECO:0000313|EMBL:EHJ07587.1,
RC ECO:0000313|Proteomes:UP000005413};
RX PubMed=22272658; DOI=10.1186/1471-2164-13-38;
RA Suzuki H., Lefebure T., Pavinski Bitar P., Stanhope M.J.;
RT "Comparative genomic analysis of the genus Staphylococcus including
RT Staphylococcus aureus and its newly described sister species Staphylococcus
RT simiae.";
RL BMC Genomics 13:38-38(2012).
CC -!- FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to D-
CC ribitol 5-phosphate. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_02068};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02068}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. TarI
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02068}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02068}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHJ07587.1}.
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DR EMBL; AEUN01000459; EHJ07587.1; -; Genomic_DNA.
DR RefSeq; WP_002464435.1; NZ_AEUN01000459.1.
DR AlphaFoldDB; G5JJT0; -.
DR PATRIC; fig|911238.3.peg.1513; -.
DR OrthoDB; 9806837at2; -.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000005413; Unassembled WGS sequence.
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 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 PANTHER; PTHR32125; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR32125:SF8; RIBITOL-5-PHOSPHATE CYTIDYLYLTRANSFERASE; 1.
DR Pfam; PF01128; IspD; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS01295; ISPD; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02068};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_02068,
KW ECO:0000313|EMBL:EHJ07587.1};
KW Teichoic acid biosynthesis {ECO:0000256|ARBA:ARBA00022944,
KW ECO:0000256|HAMAP-Rule:MF_02068};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02068, ECO:0000313|EMBL:EHJ07587.1}.
FT BINDING 7..10
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02068"
FT BINDING 81..87
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02068"
FT SITE 14
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02068"
FT SITE 22
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02068"
FT SITE 160
FT /note="Positions ribitol 5-phosphate for the nucleophilic
FT attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02068"
FT SITE 217
FT /note="Positions ribitol 5-phosphate for the nucleophilic
FT attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02068"
SQ SEQUENCE 238 AA; 26764 MW; 43316E47D96AF9BA CRC64;
MIYAGILAGG IGSRMGNVPL PKQFLDLDGK PILIHTIEKF MLVSDFDKIF IATPQKWVSH
TKDILRKHHI HDDRIEVVQG GTDRNETIMN IIHEIEHRQP ITDDDVIITH DAVRPFLTHR
IIKENIDSVL KYGAVDTVIS ATDTIVTSTD GECVHTIPVR NDMYQGQTPQ SFNIKLLRNS
YSALSAEQKD ILTDACKILI VADQQVRLVR GELYNIKITT PYDLKVANSI LKGGMLND
//
