ID   TAGX_STAA8              Reviewed;         353 AA.
AC   O05154; Q2G2X3;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Putative glycosyltransferase TagX;
DE            EC=2.4.-.-;
DE   AltName: Full=Teichoic acid biosynthesis protein X;
GN   Name=tagX; OrderedLocusNames=SAOUHSC_00644;
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 [GENOMIC DNA].
RA   Bayles K.W.;
RT   "The Staphylococcus aureus teichoic acid biosynthesis genes.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
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).
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB51062.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U91741; AAB51062.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000253; ABD29779.1; -; Genomic_DNA.
DR   RefSeq; WP_001212874.1; NZ_LS483365.1.
DR   RefSeq; YP_499204.1; NC_007795.1.
DR   AlphaFoldDB; O05154; -.
DR   SMR; O05154; -.
DR   STRING; 1280.SAXN108_0708; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; ABD29779; ABD29779; SAOUHSC_00644.
DR   GeneID; 3919936; -.
DR   KEGG; sao:SAOUHSC_00644; -.
DR   PATRIC; fig|93061.5.peg.578; -.
DR   eggNOG; COG1216; Bacteria.
DR   HOGENOM; CLU_067098_0_0_9; -.
DR   OMA; VFCEEHT; -.
DR   PRO; PR:O05154; -.
DR   Proteomes; UP000008816; 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:0045226; P:extracellular polysaccharide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0044010; P:single-species biofilm formation; IBA:GO_Central.
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   Reference proteome; Teichoic acid biosynthesis; Transferase.
FT   CHAIN           1..353
FT                   /note="Putative glycosyltransferase TagX"
FT                   /id="PRO_0000059222"
SQ   SEQUENCE   353 AA;  41139 MW;  FB6B71D63226041D CRC64;
     MRFTIIIPTC NNEATIRQLL ISIESKEHYR ILCIDGGSTD QTIPMIERLQ RELKHISLIQ
     LQNASIATCI NKGLMDIKMT DPHDSDAFMV IKPTSIVLPG KLDRLTAAFK NNDNIDMVIG
     QRAYNYHGEW KLKSADEFIK DNRIVTLTEQ PDLLSMMSFD GKLFSAKFAE LQCDETLANT
     YNHAILVKAM QKATDIHLVS QMIVGDNDID THATSNDEDF NRYITEIMKI RQRVMEMLLL
     PEQRLLYSDM VDRILFNNSL KYYMNEHPAV THTTIQLVKD YIMSMQHSDY VSQNMFDIIN
     TVEFIGENWD REIYELWRQT LIQVGINRPT YKKFLIQLKG RKFAHRTKSM LKR