TAGX_STAAS
ID TAGX_STAAS Reviewed; 353 AA.
AC Q6GBJ0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Putative glycosyltransferase TagX;
DE EC=2.4.-.-;
DE AltName: Full=Teichoic acid biosynthesis protein X;
GN Name=tagX; OrderedLocusNames=SAS0606;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571857; CAG42381.1; -; Genomic_DNA.
DR RefSeq; WP_001241175.1; NC_002953.3.
DR AlphaFoldDB; Q6GBJ0; -.
DR SMR; Q6GBJ0; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR KEGG; sas:SAS0606; -.
DR HOGENOM; CLU_067098_0_0_9; -.
DR OMA; VFCEEHT; -.
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_0000059227"
SQ SEQUENCE 353 AA; 41089 MW; 6285BA7EFC519E23 CRC64;
MRLTIIIPTC NNEATIRQLL ISIESKEHYR ILCIDGGSTD QTIPMIERLP RELKHISLIQ
LQNASIATCI NKGLMDIKMT DPHDSDAFMV INPTSIVLPG KLDRLTAAFK NNDNIDMVIG
QRAYNYHGEW KLKSADEFIK DNRIVTLTEQ PDLLSMMSFD GKLFSAKFAE LQCDETLANT
YNHTILVKAM QKATDIHLVS QMIVGDNDID THATSNDEDF NRYITEIMKI RQRVMEMLLL
PEQRLLYSDM VDRILFNNSL KYYMNEHPAV THTTIQLVKD YIMSMQHSDY VSQNMFDIIN
TVEFIGENWD REIYELWRQT LIQVGINRPT YKKFLIQLKG RKFAHRTKSM LKR