TAGX_STAAN
ID TAGX_STAAN Reviewed; 353 AA.
AC Q7A711;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Putative glycosyltransferase TagX;
DE EC=2.4.-.-;
DE AltName: Full=Teichoic acid biosynthesis protein X;
GN Name=tagX; OrderedLocusNames=SA0596;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB41828.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000018; BAB41828.1; ALT_INIT; Genomic_DNA.
DR PIR; A89834; A89834.
DR RefSeq; WP_001241182.1; NC_002745.2.
DR AlphaFoldDB; Q7A711; -.
DR SMR; Q7A711; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; BAB41828; BAB41828; BAB41828.
DR KEGG; sau:SA0596; -.
DR HOGENOM; CLU_067098_0_0_9; -.
DR Proteomes; UP000000751; 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 1: Evidence at protein level;
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_0000059225"
SQ SEQUENCE 353 AA; 41103 MW; 1E3C6CEE803AF3B3 CRC64;
MRLTIIIPTC NNEATIRQLL ISIESKEHYR ILCIDGGSTD QTIPMIERLQ RELKHISLIQ
LQNASIATCI NKGLMDIKMT DPHDSDAFMV INPTSIVLPG KLDRLTAAFK NNDNIDMVIG
QRAYNYHGEW KLKSADEFIK DNRIVTLTEQ PDLLSMMSFD GKLFSAKFAE LQCDETLANT
YNHAILVKAM QKATDIHLVS QMIVGDNDID THATSNDEDF NRYIIEIMKI RQRVMEMLLL
PEQRLLYSDM VDRILFNNSL KYYMNEHPAV THTTIQLVKD YIMSMQHSDY VSQNMFDIIN
TVEFIGENWD REIYELWRQT LIQVGINRPT YKKFLIQLKG RKFAHRTKSM LKR