ID   TARB_STAA8              Reviewed;         367 AA.
AC   Q2G2X4;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Teichoic acid glycerol-phosphate primase {ECO:0000305};
DE            EC=2.7.8.44 {ECO:0000269|PubMed:18215769};
DE   AltName: Full=CDP-glycerol:N-acetyl-beta-D-mannosaminyl-1,4-N-acetyl-D-glucosaminyldiphosphoundecaprenyl glycerophosphotransferase;
DE   AltName: Full=Tag primase {ECO:0000305};
GN   Name=tarB; OrderedLocusNames=SAOUHSC_00643 {ECO:0000312|EMBL:ABD29778.1};
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47 {ECO:0000312|Proteomes:UP000008816};
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=NCTC 8325 / PS 47;
RX   PubMed=18215769; DOI=10.1016/j.chembiol.2007.11.011;
RA   Brown S., Zhang Y.H., Walker S.;
RT   "A revised pathway proposed for Staphylococcus aureus wall teichoic acid
RT   biosynthesis based on in vitro reconstitution of the intracellular steps.";
RL   Chem. Biol. 15:12-21(2008).
CC   -!- FUNCTION: Catalyzes the addition of a single glycerol phosphate residue
CC       to the prenoldiphosphate-linked disaccharide.
CC       {ECO:0000269|PubMed:18215769}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP-glycerol + N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-
CC         alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate = 4-
CC         O-[(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-
CC         acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl
CC         diphosphate + CMP + H(+); Xref=Rhea:RHEA:33815, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58311, ChEBI:CHEBI:60377, ChEBI:CHEBI:132210,
CC         ChEBI:CHEBI:132211; EC=2.7.8.44;
CC         Evidence={ECO:0000269|PubMed:18215769};
CC   -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC       biosynthesis. {ECO:0000305|PubMed:18215769}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P27621};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P27621}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:P27621}.
CC   -!- SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase
CC       family. {ECO:0000305}.
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DR   EMBL; CP000253; ABD29778.1; -; Genomic_DNA.
DR   RefSeq; WP_001101603.1; NZ_LS483365.1.
DR   RefSeq; YP_499203.1; NC_007795.1.
DR   AlphaFoldDB; Q2G2X4; -.
DR   SMR; Q2G2X4; -.
DR   STRING; 1280.SAXN108_0707; -.
DR   EnsemblBacteria; ABD29778; ABD29778; SAOUHSC_00643.
DR   GeneID; 3920051; -.
DR   KEGG; sao:SAOUHSC_00643; -.
DR   PATRIC; fig|93061.5.peg.577; -.
DR   eggNOG; COG1887; Bacteria.
DR   HOGENOM; CLU_029598_0_1_9; -.
DR   OMA; QVWHANG; -.
DR   BioCyc; MetaCyc:MON-19983; -.
DR   BRENDA; 2.7.8.44; 3352.
DR   UniPathway; UPA00790; -.
DR   Proteomes; UP000008816; 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   Reference proteome; Teichoic acid biosynthesis; Transferase.
FT   CHAIN           1..367
FT                   /note="Teichoic acid glycerol-phosphate primase"
FT                   /id="PRO_0000438713"
SQ   SEQUENCE   367 AA;  42436 MW;  A218CE6D2FFB4489 CRC64;
     MNVLIKKFYH LVVRILSKMI TPQVIDKPHI VFMMTFPEDI KPIIKALNNS SYQKTVLTTP
     KQAPYLSELS DDVDVIEMTN RTLVKQIKAL KSAQMIIIDN YYLLLGGYNK TSNQHIVQTW
     HASGALKNFG LTDHQVDVSD KAMVQQYRKV YQATDFYLVG CEQMSQCFKQ SLGATEEQML
     YFGLPRINKY YTADRATVKA ELKDKYGITN KLVLYVPTYR EDKADNRAID KAYFEKCLPG
     YTLINKLHPS IEDSDIDDVS SIDTSTLMLM SDIIISDYSS LPIEASLLDI PTIFYVYDEG
     TYDQVRGLNQ FYKAIPDSYK VYTEEDLIMT IQEKEHLLSP LFKDWHKYNT DKSLHQLTEY
     IDKMVTK