ID   TARF_STAA8              Reviewed;         389 AA.
AC   Q2G1C1;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Teichoic acid glycerol-phosphate transferase {ECO:0000305};
DE            EC=2.7.8.45 {ECO:0000269|PubMed:18215769};
GN   Name=tarF; OrderedLocusNames=SAOUHSC_00223 {ECO:0000312|EMBL:ABD29399.1};
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 second glycerol phosphate unit
CC       from CDP-glycerol to the prenolpyrophosphate-linked disaccharide, to
CC       complete the linkage unit. {ECO:0000269|PubMed:18215769}.
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-glycerol = 4-O-[di(2R)-glycerylphospho]-N-acetyl-
CC         beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-
CC         trans,octa-cis-undecaprenyl diphosphate + CMP + H(+);
CC         Xref=Rhea:RHEA:50880, ChEBI:CHEBI:15378, ChEBI:CHEBI:58311,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:132211, ChEBI:CHEBI:133867;
CC         EC=2.7.8.45; 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: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; CP000253; ABD29399.1; -; Genomic_DNA.
DR   RefSeq; WP_000594815.1; NZ_LS483365.1.
DR   RefSeq; YP_498819.1; NC_007795.1.
DR   AlphaFoldDB; Q2G1C1; -.
DR   SMR; Q2G1C1; -.
DR   STRING; 1280.SAXN108_0234; -.
DR   EnsemblBacteria; ABD29399; ABD29399; SAOUHSC_00223.
DR   GeneID; 3920299; -.
DR   KEGG; sao:SAOUHSC_00223; -.
DR   PATRIC; fig|93061.5.peg.205; -.
DR   eggNOG; COG1887; Bacteria.
DR   HOGENOM; CLU_029598_1_1_9; -.
DR   OMA; EPWPSSH; -.
DR   BioCyc; MetaCyc:MON-19977; -.
DR   BRENDA; 2.7.8.45; 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..389
FT                   /note="Teichoic acid glycerol-phosphate transferase"
FT                   /id="PRO_0000438783"
SQ   SEQUENCE   389 AA;  45961 MW;  385A43CA33A409A6 CRC64;
     MIKNTIKKLI EHSIYTTFKL LSKLPNKNLI YFESFHGKQY SDNPKALYEY LTEHSDAQLI
     WGVKKGYEHI FQQHNVPYVT KFSMKWFLAM PRAKAWMINT RTPDWLYKSP RTTYLQTWHG
     TPLKKIGLDI SNVKMLGTNT QNYQDGFKKE SQRWDYLVSP NPYSTSIFQN AFHVSRDKIL
     ETGYPRNDKL SHKRNDTEYI NGIKTRLNIP LDKKVIMYAP TWRDDEAIRE GSYQFNVNFD
     IEALRQALDD DYVILLRMHY LVVTRIDEHD DFVKDVSDYE DISDLYLISD ALVTDYSSVM
     FDFGVLKRPQ IFYAYDLDKY GDELRGFYMD YKKELPGPIV ENQTALIDAL KQIDETANEY
     IEARTVFYQK FCSLEDGQAS QRICQTIFK