ID   TAGX_STAAR              Reviewed;         353 AA.
AC   Q6GJ30;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Putative glycosyltransferase TagX;
DE            EC=2.4.-.-;
DE   AltName: Full=Teichoic acid biosynthesis protein X;
GN   Name=tagX; OrderedLocusNames=SAR0650;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG39667.1; -; Genomic_DNA.
DR   RefSeq; WP_001241200.1; NC_002952.2.
DR   AlphaFoldDB; Q6GJ30; -.
DR   SMR; Q6GJ30; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   KEGG; sar:SAR0650; -.
DR   HOGENOM; CLU_067098_0_0_9; -.
DR   OMA; VFCEEHT; -.
DR   OrthoDB; 865276at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; 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   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Teichoic acid biosynthesis; Transferase.
FT   CHAIN           1..353
FT                   /note="Putative glycosyltransferase TagX"
FT                   /id="PRO_0000059226"
SQ   SEQUENCE   353 AA;  41175 MW;  5B064879073E618D CRC64;
     MRLTIIIPTC NNEATIRQLL ISIESKEHYR ILCIDGGSTD QTIPMIERLQ RELKHISLIQ
     LQNASIATCI NKGLMEIKMT DPHDSDAFMV INPTSIVLPG KLDRLTAAFK NNDNIDMVIG
     QRAYNYHGEW KLKSADEFIK DNRIVTLTEQ PDLLSMMSFD GKLFSAKFAE LQCDVTLANT
     YNHEILVKAM QKATDIHLVS QMIVGDNDID THATSNNEDF KRYITEIMKI RQRVMEMLLL
     PEQRLLYSDM VDRILFNNSL KYYMNEHPAV THTTIQLVKD YIMSMQHSDY VSQNMFDIIN
     TVEFNGENWD REIYELWRQT LIQVGINRPT YKRFLIQLKG RKFAHRTKSM LKR