ID   TARF_BACSH              Reviewed;         394 AA.
AC   Q8RKI5; B7ZDL1; E0U4X3;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Teichoic acid poly(glycerol phosphate) polymerase {ECO:0000305};
DE            EC=2.7.8.12 {ECO:0000269|PubMed:21035733};
GN   Name=tarF; OrderedLocusNames=BSUW23_17545;
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, DISRUPTION PHENOTYPE, AND INDUCTION.
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 further 2-8 glycerol phosphate
CC       units from CDP-glycerol to the single glycerol phosphate unit bound to
CC       the prenolpyrophosphate-linked disaccharide. The function in the cell
CC       is unknown since the product is not part of the poly(ribitol phosphate)
CC       teichoic acid found in the cell walls. {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 + n CDP-glycerol = 4-O-{[(2R)-1-glycerylphospho](n)-(2R)-
CC         1-glycerylphospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-
CC         alpha-D-glucosaminyl undecaprenyl diphosphate + n CMP + n H(+);
CC         Xref=Rhea:RHEA:13565, Rhea:RHEA-COMP:12597, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58311, ChEBI:CHEBI:60377, ChEBI:CHEBI:132211,
CC         ChEBI:CHEBI:132224; EC=2.7.8.12;
CC         Evidence={ECO:0000269|PubMed:21035733};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: The gene is not expressed under normal growth conditions.
CC       {ECO:0000269|PubMed:21035733}.
CC   -!- DISRUPTION PHENOTYPE: No effect. {ECO:0000269|PubMed:21035733}.
CC   -!- SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase
CC       family. {ECO:0000305}.
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DR   EMBL; AJ313428; CAC86113.1; -; Genomic_DNA.
DR   EMBL; AM260209; CAJ97400.1; -; Genomic_DNA.
DR   EMBL; CP002183; ADM39544.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RKI5; -.
DR   SMR; Q8RKI5; -.
DR   PRIDE; Q8RKI5; -.
DR   EnsemblBacteria; ADM39544; ADM39544; BSUW23_17545.
DR   KEGG; bss:BSUW23_17545; -.
DR   HOGENOM; CLU_029598_1_1_9; -.
DR   OMA; LHTAKIW; -.
DR   BioCyc; MetaCyc:MON-19963; -.
DR   Proteomes; UP000002233; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047355; F:CDP-glycerol glycerophosphotransferase activity; IEA:UniProtKB-EC.
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; Membrane; Teichoic acid biosynthesis; Transferase.
FT   CHAIN           1..394
FT                   /note="Teichoic acid poly(glycerol phosphate) polymerase"
FT                   /id="PRO_0000208449"
SQ   SEQUENCE   394 AA;  47432 MW;  B9E4599F58A9A735 CRC64;
     MKSKILMKYR SLLVRIYSIV FRIIGLLPRN EKLIIFESYS GKQFSCNPRA IFEYLEENKD
     KYDYQLIWSI DKRNKDLFDN SDVNYLRRFS LKWLWYMATA KYWVTNSRLP LWIPKPRNTT
     YVQTWHGTPL KKLANDMDEV HMPGTTTEQY KRNFLKEASK WDYLISPNAY STEIFRSAFQ
     FKKTFIESGY PRNDFLHKKN RNEEMLKIKE RLGINKDKKI ILYAPTWRDN SFYAKGKYKF
     NMVLDLESLK NQLCNEYILI LRMHYLVSEN INLTEYKEFA YDFSDHNDIR ELYLISDILI
     TDYSSVFFDF AGLKRPILFY VPDIEFYRDN LRGFYYDFEK CAPGPLLKTT EKVIEAIHKT
     KNYKQDENIT SFYDQFCYLE KGDSSKKVVE ELLG