ID   TARK_BACSH              Reviewed;         389 AA.
AC   Q8RKJ1; B7ZDK5; E0U4X9;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Teichoic acid ribitol-phosphate primase {ECO:0000305};
DE            EC=2.7.8.46 {ECO:0000269|PubMed:21035733};
DE   AltName: Full=Tar primase;
GN   Name=tarK; OrderedLocusNames=BSUW23_17575;
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].
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).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=21035733; DOI=10.1016/j.chembiol.2010.07.017;
RA   Brown S., Meredith T., Swoboda J., Walker S.;
RT   "Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall
RT   teichoic acids using different enzymatic pathways.";
RL   Chem. Biol. 17:1101-1110(2010).
CC   -!- FUNCTION: Catalyzes the addition of a single ribitol phosphate unit
CC       onto the glycerol phosphate of the linkage unit, as a primer for
CC       polymerisation by TarL. {ECO:0000269|PubMed:21035733}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-O-[(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-
CC         (1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl
CC         diphosphate + CDP-L-ribitol = 4-O-[1-D-ribitylphospho-(2R)-1-
CC         glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-
CC         D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + CMP +
CC         H(+); Xref=Rhea:RHEA:50912, ChEBI:CHEBI:15378, ChEBI:CHEBI:57608,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:132211, ChEBI:CHEBI:133892;
CC         EC=2.7.8.46; Evidence={ECO:0000269|PubMed:21035733};
CC   -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC       biosynthesis. {ECO:0000269|PubMed:21035733}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase
CC       family. {ECO:0000305}.
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DR   EMBL; AJ313428; CAC86107.1; -; Genomic_DNA.
DR   EMBL; AM260209; CAJ97394.1; -; Genomic_DNA.
DR   EMBL; CP002183; ADM39550.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RKJ1; -.
DR   SMR; Q8RKJ1; -.
DR   EnsemblBacteria; ADM39550; ADM39550; BSUW23_17575.
DR   KEGG; bss:BSUW23_17575; -.
DR   HOGENOM; CLU_029598_0_0_9; -.
DR   OMA; HAHTEED; -.
DR   BioCyc; MetaCyc:MON-19964; -.
DR   BRENDA; 2.7.8.46; 14099.
DR   UniPathway; UPA00790; -.
DR   Proteomes; UP000002233; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047355; F:CDP-glycerol glycerophosphotransferase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.11820; -; 1.
DR   Gene3D; 3.40.50.12580; -; 1.
DR   InterPro; IPR007554; Glycerophosphate_synth.
DR   InterPro; IPR043148; TagF_C.
DR   InterPro; IPR043149; TagF_N.
DR   Pfam; PF04464; Glyphos_transf; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell wall biogenesis/degradation; Membrane;
KW   Teichoic acid biosynthesis; Transferase.
FT   CHAIN           1..389
FT                   /note="Teichoic acid ribitol-phosphate primase"
FT                   /id="PRO_0000208450"
FT   CONFLICT        258..259
FT                   /note="MR -> IG (in Ref. 1; CAC86107 and 2; CAJ97394)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   389 AA;  44980 MW;  0351ABFE219C132C CRC64;
     MKTFLTRIVK GVFGTAYKLL SALLPVQHDK VVIASYREDQ LSDNFRGVYE KLKQDPSLRI
     TLLFRKMDKG LIGRAAYLLH LFCSLYHLAT CRVLLLDDYY FPLYVVPKRK ETVAIQLWHA
     CGAFKKFGYS IVNKPFGPSS DYLKIVPVHS NYDYAIVSAP AAVPHFAEAF QMEEKQILPL
     GIPRTDYFYH KEHIRTVLDE FHQAYPELKH KKKLLYAPTF RGSGHHQEGD ATPLDLLQLK
     SALHHKDYVV MLHLHPYMRK HAHTEEDDFV LDLTDSYSLY DLMAISDGLI TDYSSVIFEY
     SLLKRPMYFY CPDLEDYLKE RDFYYPFESF VPGPISKDVP SLVHDIESDH EADTKRIEAF
     SQTYITHQDG KSSERVADFI SSFLTSGAD