ID   TARQ_BACSH              Reviewed;         634 AA.
AC   E0U4V7;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Poly(ribitol-phosphate) beta-glucosyltransferase {ECO:0000305};
DE            EC=2.4.1.53 {ECO:0000269|PubMed:23027967};
DE   AltName: Full=WTA beta-O glucose transferase {ECO:0000303|PubMed:23027967};
GN   Name=tarQ {ECO:0000312|EMBL:ADM39528.1};
GN   OrderedLocusNames=BSUW23_17465 {ECO:0000312|EMBL:ADM39528.1};
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 [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   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=23027967; DOI=10.1073/pnas.1209126109;
RA   Brown S., Xia G., Luhachack L.G., Campbell J., Meredith T.C., Chen C.,
RA   Winstel V., Gekeler C., Irazoqui J.E., Peschel A., Walker S.;
RT   "Methicillin resistance in Staphylococcus aureus requires glycosylated wall
RT   teichoic acids.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:18909-18914(2012).
CC   -!- FUNCTION: Attaches glucose residues to poly(RboP)-wall teichoic acids
CC       (WTAs). {ECO:0000269|PubMed:23027967}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-O-[(D-ribitylphospho)(n)-D-ribitylphospho-(2R)-
CC         glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-
CC         D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n UDP-
CC         alpha-D-glucose = 4-O-[(2-beta-D-glucosyl-D-ribitylphospho)(n)-D-
CC         ribitylphospho-(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-
CC         (1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl
CC         diphosphate + n H(+) + n UDP; Xref=Rhea:RHEA:10068, Rhea:RHEA-
CC         COMP:12833, Rhea:RHEA-COMP:14260, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:133894,
CC         ChEBI:CHEBI:139149; EC=2.4.1.53;
CC         Evidence={ECO:0000269|PubMed:23027967};
CC   -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC       biosynthesis. {ECO:0000269|PubMed:23027967}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene abolishes all WTA glucose
CC       modifications. {ECO:0000269|PubMed:23027967}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; CP002183; ADM39528.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0U4V7; -.
DR   SMR; E0U4V7; -.
DR   EnsemblBacteria; ADM39528; ADM39528; BSUW23_17465.
DR   KEGG; bss:BSUW23_17465; -.
DR   HOGENOM; CLU_018620_2_0_9; -.
DR   OMA; YETESKD; -.
DR   BioCyc; MetaCyc:MON-19974; -.
DR   UniPathway; UPA00790; -.
DR   Proteomes; UP000002233; Chromosome.
DR   GO; GO:0047266; F:poly(ribitol-phosphate) beta-glucosyltransferase activity; IEA:UniProtKB-EC.
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; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR041038; TarS_C1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF18674; TarS_C1; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Teichoic acid biosynthesis; Transferase.
FT   CHAIN           1..634
FT                   /note="Poly(ribitol-phosphate) beta-glucosyltransferase"
FT                   /id="PRO_0000446276"
SQ   SEQUENCE   634 AA;  73226 MW;  D7E1E27509D96CCE CRC64;
     MKISIVIPVY NSEDLISECL DSLVNQTMPK EDYEIICVDD KSTDSSLDIL NQYKKKYENV
     VVIERTVNSG GPGAPRNDAI KIAKGEYILF VDSDDYIGSE ALLRWYNFSK ENQSDITLGK
     LKGINGRGVP KSMFKETNPD VDLVDSKIVF TLGPQKLFKA SLLKENKITF PTHIKAAEDQ
     VFTMNAYLKA KKISVSADYD YYYLVKRDGE HMSVAYVPPE NFYGAMEDII SAIKASDLEE
     ARKIKLMAVF LNRHFDFSRT KNVTIKMKTD EERAEWFRYL SSFIHAVPEE ADQFVLPHIK
     LRLLFIRNND LRGLTQYERE EQDIKKFCTV NNGELIARYP SLERYSISEE LLKVNYKNKL
     EHYLQNIEFS DHSLSIQGTI THKLLDDETN KNQSLTGVFV HRDTKAEKYI APASYDNSTF
     TFECKFDELA SAEEDLGVWD FFIESSIDGY KLRARIGNKR AAYKYSTKTM YLGHNALFVY
     SARPYFTMNY DNLSIDIKKH AYTEAELSYE TESKDLSFIF KDKQIYLPNH SKIIVNTGQS
     EISLPVKRID LEPNCTKLTV NVQSLLEQLA HVKKERLIEF AINTSQNKIS AKVDNQAIIL
     DTKSVERKSM LFFNKMVEVQ YKLLTSKSKF YFQY