ID   TARB_BACSH              Reviewed;         383 AA.
AC   Q8RKI8; B7ZDK8; E0U4X6;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Teichoic acid glycerol-phosphate primase {ECO:0000305};
DE            EC=2.7.8.44 {ECO:0000250|UniProtKB:Q2G2X4};
DE   AltName: Full=CDP-glycerol:N-acetyl-beta-D-mannosaminyl-1,4-N-acetyl-D-glucosaminyldiphosphoundecaprenyl glycerophosphotransferase;
DE   AltName: Full=Tag primase;
GN   Name=tarB; OrderedLocusNames=BSUW23_17560;
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], AND FUNCTION.
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).
CC   -!- FUNCTION: Catalyzes the addition of a single glycerol phosphate residue
CC       to the prenoldiphosphate-linked disaccharide.
CC       {ECO:0000303|PubMed:11882717}.
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:0000250|UniProtKB:Q2G2X4};
CC   -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC       biosynthesis.
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; AJ313428; CAC86110.1; -; Genomic_DNA.
DR   EMBL; AM260209; CAJ97397.1; -; Genomic_DNA.
DR   EMBL; CP002183; ADM39547.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RKI8; -.
DR   SMR; Q8RKI8; -.
DR   EnsemblBacteria; ADM39547; ADM39547; BSUW23_17560.
DR   KEGG; bss:BSUW23_17560; -.
DR   HOGENOM; CLU_029598_0_1_9; -.
DR   OMA; QVWHANG; -.
DR   BioCyc; MetaCyc:MON-19962; -.
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   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Membrane;
KW   Teichoic acid biosynthesis; Transferase.
FT   CHAIN           1..383
FT                   /note="Teichoic acid glycerol-phosphate primase"
FT                   /id="PRO_0000208448"
SQ   SEQUENCE   383 AA;  44562 MW;  4FCFE600911FFB7C CRC64;
     MKSWFAFFYY LFIKVIGALL FWVKLGNQVT LLVSFPDNAR AILKEYQKGH FSFPIHVLLT
     QHAKSLEKEF PELTVSVINE KHPLHICKAV FSMLNSKTVI VDNYFVLTTV LTSRPDIECI
     QVWHANGAFK RFGLKDINTQ NRSRADIRRF RKVYASFDRI VVGSEHMADI FKEFFDIKGD
     TFLRFGVPLT DAYYEARENS NDLKSKYQLP AEKKIILYAP TFRDHQFESF SLPFSEKQLQ
     HDLKGEYLLA VKLHPVMKES AELPEDSAWI KDVSDLPLAD LLKMSDLLIS DYSSVPFEFA
     LLDKPILFYT YDMEAYNRTR GLIRHYTEVI PGMPCCDSGM LLDQLKDMDK LQSEVERFSR
     EWNLYSRGNA SKQLLSYVNE KSN