ID   TARA_STAAS              Reviewed;         254 AA.
AC   Q6GBJ4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_02070};
DE            EC=2.4.1.187 {ECO:0000255|HAMAP-Rule:MF_02070};
DE   AltName: Full=N-acetylmannosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_02070};
DE   AltName: Full=UDP-N-acetylmannosamine transferase {ECO:0000255|HAMAP-Rule:MF_02070};
DE   AltName: Full=UDP-N-acetylmannosamine:N-acetylglucosaminyl pyrophosphorylundecaprenol N-acetylmannosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_02070};
GN   Name=tarA; OrderedLocusNames=SAS0602;
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   -!- FUNCTION: Catalyzes the conversion of GlcNAc-PP-undecaprenol into
CC       ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate
CC       in the de novo synthesis of teichoic acid. {ECO:0000255|HAMAP-
CC       Rule:MF_02070}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl
CC         diphosphate + UDP-N-acetyl-alpha-D-mannosamine = H(+) + N-acetyl-
CC         beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-
CC         trans,octa-cis-undecaprenyl diphosphate + UDP; Xref=Rhea:RHEA:16053,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:62959,
CC         ChEBI:CHEBI:68623, ChEBI:CHEBI:132210; EC=2.4.1.187;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02070};
CC   -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC       biosynthesis. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 26 family. TagA/TarA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_02070}.
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DR   EMBL; BX571857; CAG42377.1; -; Genomic_DNA.
DR   RefSeq; WP_000215388.1; NC_002953.3.
DR   AlphaFoldDB; Q6GBJ4; -.
DR   SMR; Q6GBJ4; -.
DR   CAZy; GT26; Glycosyltransferase Family 26.
DR   KEGG; sas:SAS0602; -.
DR   HOGENOM; CLU_063203_3_1_9; -.
DR   OMA; PWRWRRM; -.
DR   UniPathway; UPA00790; -.
DR   GO; GO:0047244; F:N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06533; Glyco_transf_WecG_TagA; 1.
DR   HAMAP; MF_02070; TagA_TarA; 1.
DR   InterPro; IPR034714; TagA_TarA.
DR   InterPro; IPR004629; WecG_TagA_CpsF.
DR   PANTHER; PTHR34136; PTHR34136; 1.
DR   Pfam; PF03808; Glyco_tran_WecG; 1.
DR   TIGRFAMs; TIGR00696; wecG_tagA_cpsF; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Teichoic acid biosynthesis; Transferase.
FT   CHAIN           1..254
FT                   /note="N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-
FT                   beta-D-mannosaminyltransferase"
FT                   /id="PRO_0000208445"
SQ   SEQUENCE   254 AA;  29133 MW;  99C014388CFED0BB CRC64;
     MTVEERSNTA KVDILGVDFD NTTMLQMVEN IKTFFANQST NNLFIVTANP EIVNYATTHQ
     AYLELINQAS YIVADGTGVV KASHRLKQPL AHRIPGIELM DECLKIAHVN HQKVFLLGAT
     NEVVEAAQYA LQQRYPNISF AHHHGYIDLE DETVVKRIKL FKPDYIFVGM GFPKQEEWIM
     THENQFESTV MMGVGGSLEV FAGAKKRAPY IFRKLNIEWI YRALIDWKRI GRLKSIPIFM
     YKIAKAKRKI KKAK